@article{Aluko2021,
author = {Aluko, Oluwaseun Olayemi and Li, Chuanzong and Wang, Qian and Liu, Haobao},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Aluko et al. - 2021 - Sucrose Utilization for Improved Crop Yields A Review Article.pdf:pdf},
journal = {International Journal of Molecular Sciences},
keywords = {aluko,c,citation,environmental factors,h,li,liu,o,photosynthetic carbon assimilation,q,source-to-sink relationship,sucrose transporters,sucrose transports,sucrose utilization,sucrose utilization for,wang},
pages = {1--29},
title = {{Sucrose Utilization for Improved Crop Yields : A Review Article}},
volume = {22},
year = {2021}
}
@article{Anur2020,
author = {Anur, Risky Mulana and Mufithah, Nurul and Sawitri, Widhi Dyah and Sakakibara, Hitoshi},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Anur et al. - 2020 - Overexpression of Sucrose Phosphate Synthase Enhanced Sucrose Content and Biomass Production in Transgenic Sugarcan.pdf:pdf},
journal = {Plants},
keywords = {biomass,soluble acid invertase,sucrose,sucrose phosphate synthase,transgenic sugarcane},
number = {200},
pages = {1--11},
title = {{Overexpression of Sucrose Phosphate Synthase Enhanced Sucrose Content and Biomass Production in Transgenic Sugarcane}},
url = {doi: 10.3390/plants9020200},
volume = {9},
year = {2020}
}
@article{Apriasti2018,
author = {Apriasti, Retnosari and Widyaningrum, Suvia and Hidayati, Weny N and Sawitri, Widhi D and Darsono, Nurmalasari},
doi = {10.1007/s11033-018-4326-1},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Apriasti et al. - 2018 - Full sequence of the coat protein gene is required for the induction of pathogen-derived resistance against sug.pdf:pdf},
isbn = {0123456789},
issn = {1573-4978},
journal = {Molecular Biology Reports},
keywords = {10,1007,3-018-4326-1,Sugarcane mosaic virus,Pathogen derived resistance,article,coat protein,contains,doi,electronic supplementary material the,full dna sequence,https,n-terminal deletion,online version of this,org,pathogen derived resistance,s1103,scmv-resistant sugarcane,sugarcane mosaic virus},
number = {6},
pages = {2749--2758},
publisher = {Springer Netherlands},
title = {{Full sequence of the coat protein gene is required for the induction of pathogen-derived resistance against sugarcane mosaic virus in transgenic sugarcane}},
volume = {45},
year = {2018}
}
@article{Barker2000,
abstract = {In leaves, sucrose uptake kinetics involve high- and low-affinity components. A family of low- and high-affinity sucrose transporters (SUT) was identified. SUT1 serves as a high-affinity transporter essential for phloem loading and long-distance transport in solanaceous species. SUT4 is a low-affinity transporter with an expression pattern overlapping that of SUT1. Both SUT1 and SUT4 localize to enucleate sieve elements of tomato. New sucrose transporter-like proteins, named SUT2, from tomato and Arabidopsis contain extended cytoplasmic domains, thus structurally resembling the yeast sugar sensors SNF3 and RGT2. Features common to these sensors are low codon bias, environment of the start codon, low expression, and lack of detectable transport activity. In contrast to LeSUT1, which is induced during the sink-to-source transition of leaves, SUT2 is more highly expressed in sink than in source leaves and is inducible by sucrose. LeSUT2 protein colocalizes with the low- and high-affinity sucrose transporters in sieve elements of tomato petioles, indicating that multiple SUT mRNAs or proteins travel from companion cells to enucleate sieve elements. The SUT2 gene maps on chromosome V of potato and is linked to a major quantitative trait locus for tuber starch content and yield. Thus, the putative sugar sensor identified colocalizes with two other sucrose transporters, differs from them in kinetic properties, and potentially regulates the relative activity of low- and high-affinity sucrose transport into sieve elements.},
author = {Barker, L.},
doi = {10.1105/tpc.12.7.1153},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Barker - 2000 - SUT2, a putative sucrose sensor in sieve elements.pdf:pdf},
isbn = {1040-4651 (Print)},
issn = {1040-4651},
journal = {the Plant Cell},
keywords = {Amino Acid Sequence,Complementary,DNA, Complementary,Fungal Proteins,Genetically Modified,Kinetics,Lycopersicon esculentum,Lycopersicon esculentum: genetics,Molecular Sequence Data,Monosaccharide Transport Proteins,Monosaccharide Transport Proteins: chemistry,Monosaccharide Transport Proteins: genetics,Monosaccharide Transport Proteins: metabolism,Plants, Genetically Modified,Saccharomyces cerevisiae,Saccharomyces cerevisiae: genetics,Sucrose,Sucrose: metabolism},
number = {7},
pages = {1153--1164},
pmid = {10899981},
title = {{SUT2, a putative sucrose sensor in sieve elements}},
volume = {12},
year = {2000}
}
@article{Castleden2004,
abstract = {Suc-phosphate synthase (SPS) is a key regulatory enzyme in the pathway of Sue biosynthesis and has been linked to quantitative trait loci controlling plant growth and yield. In dicotyledonous plants there are three SPS gene families: A, B, and C. Here we report the finding of five families of SPS genes in wheat (Triticum aestivum) and other monocotyledonous plants from the family Poaceae (grasses). Three of these form separate subfamilies within the previously described A, B, and C gene families, but the other two form a novel and distinctive D family, which on present evidence is only found in the Poaceae. The D-type SPS proteins lack the phosphorylation sites associated with 14-3-3 protein binding and osmotic stress activation, and the linker region between the N-terminal catalytic glucosyltransferase domain and the C-terminal Suc-phosphatase-like domain is 80 to 90 amino acid residues shorter than in the A, B, or C types. The D family appears to have arisen after the divergence of mono- and dicotyledonous plants, with a later duplication event resulting in the two D-type subfamilies. Each of the SPS gene families in wheat showed different, but overlapping, spatial and temporal expression patterns, and in most organs at least two different SPS genes are expressed. Analysis of expressed sequence tags indicated similar expression patterns to wheat for each SPS gene family in barley (Hordeum vulgare) but not in more distantly related grasses. We identified an expressed sequence tag from rice (Oryza sativa) that appears to be derived from an endogenous antisense SPS gene, and this might account for the apparently low level of expression of the related OsSPS11 sense gene, adding to the already extensive list of mechanisms for regulating the activity of SPS in plants.},
author = {Castleden, C. Kate and Aoki, Naohiro and Gillespie, Vanessa J. and MacRae, Elspeth A. and Quick, W. Paul and Buchner, Peter and Foyer, Christine H. and Furbank, Robert T. and Lunn, John E.},
doi = {10.1104/pp.104.042457},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Castleden et al. - 2004 - Evolution and function of the sucrose-phosphate synthase gene families in wheat and other grasses.pdf:pdf},
issn = {00320889},
journal = {Plant Physiology},
number = {3},
pages = {1753--1764},
pmid = {15247374},
title = {{Evolution and function of the sucrose-phosphate synthase gene families in wheat and other grasses}},
volume = {135},
year = {2004}
}
@article{Cumino2002,
abstract = {Based on the functional characterization of sucrose biosynthesis related proteins [SBP: sucrose-phosphate synthase (SPS), sucrose-phosphate phosphatase (SPP), and sucrose synthase (SuS)] in Anabaena sp. PCC7120 and sequence analysis, we have shown that SBP are restricted to cyanobacterium species and plants, and that they are multidomain proteins with modular architecture. Anabaena SPS, a minimal catalytic SPS unit, defines a glucosyltransferase domain present in all SPSs and SuSs. Similarly, Anabaena SPP defines a phosphohydrolase domain characteristic of all SPPs and some SPSs. Phylogenetic analysis points towards the evolution of modern cyanobacterial and plant SBP from a bidomainal common ancestral SPS-like gene. {\textcopyright} 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.},
author = {Cumino, Andrea and Curatti, Leonardo and Giarrocco, Laura and Salerno, Graciela L.},
doi = {10.1016/S0014-5793(02)02516-4},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Cumino et al. - 2002 - Sucrose metabolism Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functiona.pdf:pdf},
isbn = {0014-5793 (Print)\r0014-5793 (Linking)},
issn = {00145793},
journal = {FEBS Letters},
keywords = {Cyanobacterium,Modular arrangement,Phylogenetic analysis,Sucrose synthase,Sucrose-phosphate phosphatase,Sucrose-phosphate synthase},
number = {1-3},
pages = {19--23},
pmid = {12062401},
title = {{Sucrose metabolism: Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functional domains shuffled during evolution}},
volume = {517},
year = {2002}
}
@article{Doehlert1983,
author = {Doehlert, Douglas C. and Huber, Steven C.},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Doehlert, Huber - 1983 - Regulation of Spinach Leaf Sucrose Phosphate Synthase by Glucose-6-Phosphate , Inorganic Phosphate , and pH1.pdf:pdf},
journal = {Plant Physiol},
pages = {989--994},
title = {{Regulation of Spinach Leaf Sucrose Phosphate Synthase by Glucose-6-Phosphate , Inorganic Phosphate , and pH1}},
volume = {73},
year = {1983}
}
@article{Falter2016,
abstract = {The substitution of fossil by renewable energy sources is a major strategy in reducing CO2 emission and mitigating climate change. In the transport sector, which is still mainly dependent on liquid fuels, the production of second generation ethanol from lignocellulosic feedstock is a promising strategy to substitute fossil fuels. The main prerequisites on designated crops for increased biomass production are high biomass yield and optimized saccharification for subsequent use in fermentation processes. We tried to address these traits by the overexpression of a sucrose-phosphate synthase gene (SoSPS) from sugarcane (Saccharum officinarum) in the model grass Brachypodium distachyon. The resulting transgenic B. distachyon lines not only revealed increased plant height at early growth stages but also higher biomass yield from fully senesced plants, which was increased up to 52 % compared to wild-type. Additionally, we determined higher sucrose content in senesced leaf biomass from the transgenic lines, which correlated with improved biomass saccharification after conventional thermo-chemical pretreatment and enzymatic hydrolysis. Combining increased biomass production and saccharification efficiency in the generated B. distachyon SoSPS overexpression lines, we obtained a maximum of 74 % increase in glucose release per plant compared to wild-type. Therefore, we consider SoSPS overexpression as a promising approach in molecular breeding of energy crops for optimizing yields of biomass and its utilization in second generation biofuel production.},
author = {Falter, Christian and Voigt, Christian A.},
doi = {10.1007/s13562-015-0343-5},
issn = {09741275},
journal = {Journal of Plant Biochemistry and Biotechnology},
keywords = {Biomass,Metabolic engineering,Plant development,Saccharification,Sucrose,Transformation},
number = {3},
pages = {311--318},
publisher = {Journal of Plant Biochemistry and Biotechnology},
title = {{Improving biomass production and saccharification in Brachypodium distachyon through overexpression of a sucrose-phosphate synthase from sugarcane}},
volume = {25},
year = {2016}
}
@article{Ferreon2013,
abstract = {Allostery is an intrinsic property of many globular proteins and enzymes that is indispensable for cellular regulatory and feedback mechanisms. Recent theoretical and empirical observations indicate that allostery is also manifest in intrinsically disordered proteins, which account for a substantial proportion of the proteome. Many intrinsically disordered proteins are promiscuous binders that interact with multiple partners and frequently function as molecular hubs in protein interaction networks. The adenovirus early region 1A (E1A) oncoprotein is a prime example of a molecular hub intrinsically disordered protein. E1A can induce marked epigenetic reprogramming of the cell within hours after infection, through interactions with a diverse set of partners that include key host regulators such as the general transcriptional coactivator CREB binding protein (CBP), its paralogue p300, and the retinoblastoma protein (pRb; also called RB1). Little is known about the allosteric effects at play in E1A-CBP-pRb interactions, or more generally in hub intrinsically disordered protein interaction networks. Here we used single-molecule fluorescence resonance energy transfer (smFRET) to study coupled binding and folding processes in the ternary E1A system. The low concentrations used in these high-sensitivity experiments proved to be essential for these studies, which are challenging owing to a combination of E1A aggregation propensity and high-affinity binding interactions. Our data revealed that E1A-CBP-pRb interactions have either positive or negative cooperativity, depending on the available E1A interaction sites. This striking cooperativity switch enables fine-tuning of the thermodynamic accessibility of the ternary versus binary E1A complexes, and may permit a context-specific tuning of associated downstream signalling outputs. Such a modulation of allosteric interactions is probably a common mechanism in molecular hub intrinsically disordered protein function. {\textcopyright} 2013 Macmillan Publishers Limited. All rights reserved.},
author = {Ferreon, Allan Chris M. and Ferreon, Josephine C. and Wright, Peter E. and Deniz, Ashok A.},
doi = {10.1038/nature12294},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Ferreon et al. - 2013 - Modulation of allostery by protein intrinsic disorder.pdf:pdf},
issn = {00280836},
journal = {Nature},
number = {7454},
pages = {390--394},
pmid = {23783631},
publisher = {Nature Publishing Group},
title = {{Modulation of allostery by protein intrinsic disorder}},
volume = {498},
year = {2013}
}
@article{Hilser2007,
abstract = {Transcription factors and other allosteric cell signaling proteins contain a disproportionate number of domains or segments that are intrinsically disordered (ID) under native conditions. In many cases folding of these segments is coupled to binding with one or more of their interaction partners, suggesting that intrinsic disorder plays an important functional role. Despite numerous hypotheses for the role of ID domains in regulation, a mechanistic model has yet to be established that can quantitatively assess the importance of intrinsic disorder for intramolecular site-to-site communication, the hallmark property of allosteric proteins. Here, we present such a model and show that site-to-site allosteric coupling is maximized when intrinsic disorder is present in the domains or segments containing one or both of the coupled binding sites. This result not only explains the prevalence of ID domains in regulatory proteins, it also calls into question the classical mechanical view of energy propagation in proteins, which predicts that site-to-site coupling would be maximized when a well defined pathway of folded structure connects the two sites. Furthermore, in showing that the coupling mechanism conferred by intrinsic disorder is robust and independent of the network of interactions that physically link the coupled sites, unique insights are gained into the energetic ground rules that govern site-to-site communication in all proteins. {\textcopyright} 2007 by The National Academy of Sciences of the USA.},
author = {Hilser, Vincent J. and Thompson, E. Brad},
doi = {10.1073/pnas.0700329104},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Hilser, Thompson - 2007 - Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.pdf:pdf},
issn = {00278424},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
keywords = {Allostery,Ensemble,Regulation,Site-to-site communication},
number = {20},
pages = {8311--8315},
pmid = {17494761},
title = {{Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins}},
volume = {104},
year = {2007}
}
@article{Huber1991,
abstract = {Studies were conducted to determine the potential for regulation of maize leaf sucrose-phosphate synthase (SPS) by protein phosphorylation. Highly activated enzyme, in desalted crude leaf extracts prepared from illuminated leaves, was inactivated in vitro in a time- and ATP-de-pendent manner. Partial purification of SPS by polyethylene glycol fractionation and Mono Q chromatography yielded enzyme that was not ATP-inactivated, possibly due to elimination of contaminating protein kinase. We used the partially purified SPS as substrate to identify an endogenous protein kinase. The protein kinase catalyzed the time- and ATP-dependent inacti-vation of SPS, and the apparent Km for Mg-ATP was estimated to be approximately 10$\mu$M. The partially purified maize SPS protein was phosphorylated in vitro using [y-32P]ATP and either the endogenous protein kinase or the catalytic subunit of cAMP-dependent protein kinase. The incorporation of radiolabel was closely paralleled by inactivation of the enzyme. These results provide the first evidence for regulation of maize leaf SPS by protein phosphorylation, which we postulate is the mechanism of light-dark regulation in vivo. {\textcopyright} 1991. The Japanese Society of Plant Physiologists (JSPP).},
author = {Huber, S. C. and Huber, J. L.},
doi = {10.1093/oxfordjournals.pcp.a078083},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Huber, Huber - 1991 - Regulation of maize leaf sucrose-phosphate synthase by protein phosphorylation.pdf:pdf},
issn = {00320781},
journal = {Plant and Cell Physiology},
keywords = {Maize,Protein kinase,Protein phosphorylation,Sucrose biosynthesis,Sucrose-phosphate synthase},
number = {3},
pages = {319--326},
title = {{Regulation of maize leaf sucrose-phosphate synthase by protein phosphorylation}},
volume = {32},
year = {1991}
}
@article{Huber1996,
abstract = {Sucrose-phosphate synthase (SPS; E.C. 2.4.1.14) is the plant enzyme thought to play a major role in sucrose biosynthesis. In photosynthetic and nonphotosynthetic tissues, SPS is regulated by metabolites and by reversible protein phosphorylation. In leaves, phosphorylation modulates SPS activity in response to light/dark signals and end-product accumulation. SPS is phosphorylated on multiple seryl residues in vivo, and the major regulatory phosphorylation site involved is Ser158 in spinach leaves and Ser162 in maize leaves. Regulation of the enzymatic activity of SPS appears to involve calcium, metabolites, and novel "coarse" control of the protein phosphatase that activates SPS. Activation of SPS also occurs during osmotic stress of leaf tissue in darkness, which may function to facilitate sucrose formation for osmoregulation. Manipulation of SPS expression in vivo confirms the role of this enzyme in the control of sucrose biosynthesis.},
author = {Huber, Steven C. and Huber, Joan L.},
doi = {10.1146/annurev.arplant.47.1.431},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Huber, Huber - 1996 - Role and Regulation of Sucrose-Phosphate Synthase in Higher Plants.pdf:pdf},
isbn = {0066-4294},
issn = {1040-2519},
journal = {Annual Review of Plant Physiology and Plant Molecular Biology},
keywords = {maize,protein kinase,regula-,spinach,spinacia oleracea l,sucrose synthesis,tory protein phosphorylation,zea mays l},
number = {1},
pages = {431--444},
pmid = {15012296},
title = {{Role and Regulation of Sucrose-Phosphate Synthase in Higher Plants}},
volume = {47},
year = {1996}
}
@article{Huber1994,
author = {Huber, Steven C and Huber, Joan L and Mcmichael, Robert W},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Huber, Huber, Mcmichael - 1994 - Control of Plant Enzyme Activity by Reversible Protein Phosphorylation.pdf:pdf},
journal = {International Review of Citology},
pages = {47--97},
title = {{Control of Plant Enzyme Activity by Reversible Protein Phosphorylation}},
volume = {149},
year = {1994}
}
@article{Ishimaru2008,
abstract = {We analyzed the yield characters of field-grown transgenic potato plants (Solanum tuberosum) carrying a maize gene for sucrose-phosphate synthase (SPS), the key enzyme in sucrose synthesis. The SPS activity in the leaves of transgenic plants (line Ag1203) was 2 times that of the control (cv. May Queen). There was no difference in the photosynthetic CO2 uptake rates between Ag1203 and May Queen plants, and the leaf starch content of Ag1203 was lower. These observations indicate that the introduction of a foreign SPS gene improved the supply of photosynthate from source (leaves) to sink (tubers). Additionally, leaf senescence of the transgenic potato plants was delayed relative to that of May Queen. The average tuber weight and total yield of Ag1203 plants were at least 20% higher, and the tuber sucrose content, which is related to eating quality, was also higher. Increased translocation of photosynthate and longer period of photosynthetic activity in the leaves may have increased the yield of Ag1203. These results suggest that introduction of the SPS gene improved the yield characters and quality of potato tubers under field conditions.},
author = {Ishimaru, Ken and Hirotsu, Naoki and Kashiwagi, Takayuki and Madoka, Yuka and Nagasuga, Kiyoshi and Ono, Kiyomi and Ohsugi, Ryu},
doi = {10.1626/pps.11.104},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Ishimaru et al. - 2008 - Overexpression of a maize SPS gene improves yield characters of potato under field conditions.pdf:pdf},
issn = {1343943X},
journal = {Plant Production Science},
keywords = {Potato,SPS,Transgenic,Yield},
number = {1},
pages = {104--107},
title = {{Overexpression of a maize SPS gene improves yield characters of potato under field conditions}},
volume = {11},
year = {2008}
}
@article{Kurniah2021,
abstract = {Plant sucrose-phosphate synthase (SPS) contains a glycosyltransferase domain, which specifically catalyzes reactions with the nucleotide sugar uridine diphosphate glucose (UDP-G) as a donor substrate. Unlike plant SPS, bacterial SPS is predicted to bind other nucleotide sugars, such as adenosine diphosphate glucose (ADP-G). This study aimed to identify the UDP-G binding site of sugarcane (Saccharum officinarum) SPS (SoSPS1) and to improve its affinity for ADP-G by site-directed mutagenesis. To achieve targeted mutagenesis, amino acid distribution and comparative modeling studies were performed, followed by site-directed mutagenesis of SoSPS1 in the putative UDP-G binding motif. The N-terminal deletion of SoSPS1 (∆N-SoSPS1) was used for enzymatic analysis. The results showed that mutations in the R-X4-K, E-X7-E, and H-X5-V motifs significantly affect UDP-G and ADP-G binding. Mutations at R496 and K501 severely attenuate the affinity for UDP-G. Additionally, alanine substitutions at E591 and V570 decreased the UDP-G affinity but remarkably increased its ADP-G affinity. The R-X4-K motif plays a crucial role in the UDP-G binding site and catalytic activity of plant SPS; thus, its alteration to other amino acids was not viable. The E-X7-E and H-X5-V motifs may bind to the nucleotide glucose substrate, indicating that these motifs are involved in substrate specificity. These results agree with substrate docking simulations at the mutated residue positions, supporting the experimental results. These results demonstrate that mutation of E591 and V570 severely attenuated the UDP-G affinity, while retaining its activity against ADP-G, offering strategic insights into increasing sucrose synthesis and plant growth.},
author = {Kurniah, Nuriyah Inda and Sawitri, Widhi Dyah and Rohman, Muhammad Saifur and Nugraha, Yudhi and Hase, Toshiharu and Sugiharto, Bambang},
doi = {10.1007/s11033-021-06181-8},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Kurniah et al. - 2021 - Mutation of UDP-glucose binding motif residues lead to increased affinity for ADP-glucose in sugarcane sucrose p.pdf:pdf},
isbn = {0123456789},
issn = {15734978},
journal = {Molecular Biology Reports},
keywords = {Adenine diphosphate glucose,Glycosyltransferase,Site-directed mutagenesis,Sucrose phosphate synthase,Uridine diphosphate glucose},
number = {2},
pages = {1697--1706},
publisher = {Springer Netherlands},
title = {{Mutation of UDP-glucose binding motif residues lead to increased affinity for ADP-glucose in sugarcane sucrose phosphate synthase}},
volume = {48},
year = {2021}
}
@article{Laemmli1970,
author = {Laemmli, U K},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Laemmli - 1970 - Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4.pdf:pdf},
journal = {Nature},
pages = {680--685},
title = {{Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4}},
volume = {227},
year = {1970}
}
@article{Lunn2003,
abstract = {Sucrose-phosphate synthase (SPS) from the cyanobacterium Synechocystis sp. PCC 6803 lacks all of the Ser residues known to be involved in the regulation of higher plant SPS by protein phosphorylation. The Synechocystis SPS is also not allosterically regulated by glucose 6-phosphate or orthophosphate. To investigate the effects of expressing a potentially unregulated SPS in plants, the Synechocystis sps gene was introduced into tobacco, rice and tomato under the control of constitutive promoters. The Synechocystis SPS protein was expressed at a high level in the plants, which should have been sufficient to increase overall SPS activity 2-8-fold in the leaves. However, SPS activities and carbon partitioning in leaves from transgenic and wild-type plants were not significantly different. The maximal light-saturated rates of photosynthesis in leaves from tomato plants expressing the Synechocystis SPS were the same as those from wild-type plants. Tomato plants expressing the maize SPS showed 2-3-fold increases in SPS activity, increased partitioning of photoassimilate to sucrose and up to 58% higher maximal rates of photosynthesis. To investigate the apparent inactivity of the Synechocystis SPS the enzyme was purified from transgenic tobacco and rice plants. Surprisingly, the purified enzyme was found to have full catalytic activity. It is proposed that some other protein in plant cells binds to the Synechocystis SPS resulting in inhibition of the enzyme.},
author = {Lunn, John E. and Gillespie, Vanessa J. and Furbank, Robert T.},
doi = {10.1093/jxb/erg023},
issn = {00220957},
journal = {Journal of Experimental Botany},
keywords = {Carbon partitioning,Lycopersicon esculentum Mill.,Nicotiana tabacum L.,Oryza sativa L.,Photosynthesis,Rice,Sucrose-phosphate synthase,Synechocystis sp. PCC 6803,Tobacco,Tomato},
number = {381},
pages = {223--237},
pmid = {12493850},
title = {{Expression of a cyanobacterial sucrose-phosphate synthase from Synechocystis sp. PCC 6803 in transgenic plants}},
volume = {54},
year = {2003}
}
@article{Lunn1999,
abstract = {Sucrose is one of several low-molecular-weight compounds that cyanobacteria accumulate in response to osmotic stress and which are believed to act as osmoprotectants. The genome of the cyanobacterium Synechocystis sp. PCC 6803 contains a 2163 bp open reading frame (ORF) that shows similarity to genes from higher plants encoding sucrose-phosphate synthase (SPS), the enzyme responsible for sucrose synthesis. The deduced amino acid sequence shows 35-39% identity with known higher-plant SPS sequences. The putative Synechocystis sps gene was cloned from genomic DNA by PCR amplification and expressed as a His6-tagged amino-terminal fusion protein in Escherichia coli. The expressed protein was purified and shown to be a functional SPS enzyme, confirming the identity of the ORF, which is the first sps gene to be cloned from a prokaryotic organism. The Synechocystis SPS has a molecular mass of 81.5 kDa, which is smaller than the typical higher-plant SPS subunit (117-119 kDa), and lacks the phosphorylation site motifs associated with light- and osmotic stress-induced regulation of SPS in higher plants. The enzyme has K(m) values for UDPG1c and Fru6P of 2.9 mM and 0.22 mM, respectively, with a V(max) of 17 $\mu$mol per minute per mg protein and a pH optimum of 8.5. Unlike the higher-plant enzyme, ADPG1c, CDPG1c and GDPG1c can substitute for UDPG1c as the glucosyl donor with K(m) values of 2.5, 7.2 and 1.8 mM, respectively. The enzyme is activated by Mg2+ but not by G1c6P, and is only weakly inhibited by inorganic phosphate. The purified protein was used to raise a high-titre antiserum, which recognises a low-abundance 81 kDa protein in Synechocystis sp. PCC 6803 extracts. There was no apparent increase in expression of the 81 kDa protein when the cells were exposed to moderate salt stress, and SPS activity was very low in extracts from both unstressed and salt-stressed cells. These results and the lack of evidence for sucrose accumulation in Synechocystis sp. PCC 6803 lead to the conclusion that expression of the sps gene plays no obvious role in adaptation to osmotic stress in this species.},
author = {Lunn, John E. and Price, G. Dean and Furbank, Robert T.},
doi = {10.1023/A:1006130802706},
issn = {01674412},
journal = {Plant Molecular Biology},
keywords = {Cyanobacteria,Prokaryotic,Sucrose,Sucrose-phosphate synthase,Synechocystis sp. PCC 6803},
number = {2},
pages = {297--305},
pmid = {10412908},
title = {{Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803}},
volume = {40},
year = {1999}
}
@article{Nguyen-Quoc1999,
abstract = {Sucrose unloading and sink activity were examined in tomato plants (Lycopersicon esculentum) overexpressing sucrose phosphate synthase (SPS; EC 2.3.1.14). Like the leaves, the fruit of the transformed tomato plants had elevated (2.4-fold) SPS activity. SPS overexpression in tomato fruit did not significantly change acid invertase, and only slightly reduced ADPglc ppase activity, but enhanced sucrose synthase activity by 27%. More importantly, the amount of sucrose unloaded into the fruit was considerably increased. Using [3H]- (fructosyl)-sucrose in in vitro unloading experiments with harvested 20-d-old fruit, 70% more sucrose was unloaded into the transformed fruits compared to the untransformed controls. Furthermore, the turnover of the sucrose unloaded into the fruit of transformed plants was 60% higher than that observed in the untransformed controls. Taken together, these results demonstrate that SPS overexpression increases the sink strength of transformed tomato fruit.},
author = {Nguyen-Quoc, Binh and N'Tchobo, Hyacinthe and Foyer, Christine H. and Yelle, Serge},
doi = {10.1093/jxb/50.335.785},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Nguyen-Quoc et al. - 1999 - Overexpression of sucrose phosphate synthase increases sucrose unloading in transformed tomato fruit.pdf:pdf},
issn = {00220957},
journal = {Journal of Experimental Botany},
keywords = {Carbon metabolism,Starch,Sucrose phosphate synthase (SPS),Sucrose unloading,Tomato fruit},
number = {335},
pages = {785--791},
title = {{Overexpression of sucrose phosphate synthase increases sucrose unloading in transformed tomato fruit}},
volume = {50},
year = {1999}
}
@article{Osorio2014,
abstract = {Plant growth and carbon metabolism are closely associated since carbohydrate in the form of sucrose generated by photosynthesis, provides the primary source of building blocks and energy for the production and maintenance of biomass. Regulation of carbon partitioning between source and sink tissues is important because it has a vast influence on both plant growth and development. The regulation of carbon partitioning at the whole plant level is directly linked to the cellular pathways of assimilate transport and the metabolism and allocation of sugars, mainly sucrose and hexoses in source leaves, and sink organs such as roots and fruit. By using tomato plant as a model, this review documents and discusses our current understanding of source–sink interactions from molecular to physiological perspectives focusing on those that regulate the growth and development of both vegetative and reproductive organs. It furthermore discusses the impact that environmental conditions play in maintenance of this balance in an attempt to address the link between physiological and ecological aspects of growth.},
author = {Osorio, Sonia and Ruan, Yong Ling and Fernie, Alisdair R.},
doi = {10.3389/fpls.2014.00516},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Osorio, Ruan, Fernie - 2014 - An update on source-to-sink carbon partitioning in tomato.pdf:pdf},
issn = {1664462X},
journal = {Frontiers in Plant Science},
keywords = {Carbohydrates,Carbon partitioning,Sink organs,Source organs,Tomato},
pages = {1--11},
title = {{An update on source-to-sink carbon partitioning in tomato}},
volume = {5},
year = {2014}
}
@article{Park2008,
abstract = {The objective of this study was to manipulate the intracellular pools of sucrose by differentially expressing exogenous sucrose phosphate synthase (SPS) and investigating its role in regulating plant growth and fibre development. Tobacco (Nicotiana tabacum cv. Xanthi) plants were transformed with an arabidopsis SPS gene under the regulation of the ubiquitously expressed tandem repeat of the 35S cauliflower mosaic virus promoter, and subject to growth trials and fibre characterization. It was apparent that over-expression of SPS resulted in substantially elevated concentrations of sink sucrose pools compared to wild-type plants, while source tissue sucrose pools remained the same. All transformed plants had significantly increased stem height, which was ascribed to internode elongation, and greater stem diameters, longer fibers and increased total dry biomass relative to the control plants. Difference in the chemical composition of either the storage or structural carbohydrates of the wild-type and SPS transgenic lines were only minor. The correlation between increased stem sucrose content and plant phenotypes with elevated SPS gene expression confirm a role for sucrose availability in controlling plant growth and fibre elongation. {\textcopyright} 2007 Springer Science+Business Media B.V.},
author = {Park, Ji Young and Canam, Thomas and Kang, Kyu Young and Ellis, David D. and Mansfield, Shawn D.},
doi = {10.1007/s11248-007-9090-2},
issn = {09628819},
journal = {Transgenic Research},
keywords = {Carbohydrate metabolism,Fibre development,Plant growth,Plant metabolism,Soluble carbohydrates,Sucrose,Sucrose phosphate synthase (SPS),Tobacco},
number = {2},
pages = {181--192},
pmid = {17415671},
title = {{Over-expression of an arabidopsis family A sucrose phosphate synthase (SPS) gene alters plant growth and fibre development}},
volume = {17},
year = {2008}
}
@article{Salerno2003,
abstract = {Since the discovery of sucrose biosynthesis, considerable advances have been made in understanding its regulation and crucial role in the functional biology of plants. However, important aspects of this metabolism are still an enigma. Studies in cyanobacteria and the publication of the sequences of several complete genomes have recently significantly increased our knowledge of the structures of proteins involved in sucrose metabolism and given us new insights into their origin and further evolution.},
author = {Salerno, Graciela L. and Curatti, Leonardo},
doi = {10.1016/S1360-1385(02)00029-8},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Salerno, Curatti - 2003 - Origin of sucrose metabolism in higher plants When, how and why.pdf:pdf;:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Salerno, Curatti - 2003 - Origin of sucrose metabolism in higher plants When, how and why(2).pdf:pdf},
isbn = {1360-1385},
issn = {13601385},
journal = {Trends in Plant Science},
number = {2},
pages = {63--69},
pmid = {12597872},
title = {{Origin of sucrose metabolism in higher plants: When, how and why?}},
volume = {8},
year = {2003}
}
@article{Sawitri2017,
archivePrefix = {arXiv},
arxivId = {10.1007/s12551-017-0360-9},
author = {Sawitri, Widhi Dyah and Afidah, Siti Nurul and Nakagawa, Atsushi and Hase, Toshiharu and Sugiharto, Bambang},
eprint = {s12551-017-0360-9},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Sawitri et al. - 2017 - Identification of UDP-glucose binding site in glycosyltransferase domain of sucrose phosphate synthase from suga.pdf:pdf},
journal = {Biophysical Reviews},
keywords = {Sucrose phosphate synthase,Glycosyltransferase,Uri,glycosyltransferase,site-directed,sucrose phosphate synthase,sugarcane,uridine diphosphate glucose},
number = {2},
pages = {293--298},
pmid = {29222806},
primaryClass = {10.1007},
publisher = {Biophysical Reviews},
title = {{Identification of UDP-glucose binding site in glycosyltransferase domain of sucrose phosphate synthase from sugarcane ( Saccharum officinarum ) by structure-based site-directed mutagenesis}},
volume = {10},
year = {2017}
}
@article{Sawitri2016,
abstract = {Sucrose phosphate synthase (SPS) catalyzes the transfer of glycosyl group of uridine diphosphate glucose (UDP-G) to fructose-6-phosphate (F6P) to form sucrose-6-phosphate (S6P). Plant SPS plays a key role in photosynthetic carbon metabolisms, which activity is modulated by an allosteric activator glucose-6-phosphate (G6P). We produced recombinant sugarcane SPS using Escherichia coli and Sf9 insect cells to investigate its structure-function relationship. When expressed in E. coli, two forms of SPS with different sizes appeared; the larger was comparable in size with the authentic plant enzyme and the shorter was trimmed the N-terminal 20 kDa region off. In the insect cells, only enzyme with the authentic size was produced. We purified the trimmed SPS and the full size enzyme from insect cells and found their enzymatic properties differed significantly; the full size enzyme was activated allosterically by G6P, while the trimmed one showed a high activity even without G6P. We further introduced a series of N-terminal truncations up to 171 residue and found G6P-independent activity was enhanced by the truncation. These combined results indicated that the N-terminal region of sugarcane SPS is crucial for the allosteric regulation by G6P and may function like a suppressor domain for the enzyme activity.},
author = {Sawitri, Widhi Dyah and Narita, Hirotaka and Ishizaka-Ikeda, Etsuko and Sugiharto, Bambang and Hase, Toshiharu and Nakagawa, Atsushi},
doi = {10.1093/jb/mvw004},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Sawitri et al. - 2016 - Purification and characterization of recombinant sugarcane sucrose phosphate synthase expressed in E. Coli and i.pdf:pdf},
issn = {17562651},
journal = {Journal of Biochemistry},
keywords = {Allosteric regulation,Carbon metabolism,Recombinant enzyme,Sucrose phosphate synthase,Sugarcane},
number = {6},
pages = {599--607},
title = {{Purification and characterization of recombinant sugarcane sucrose phosphate synthase expressed in E. Coli and insect Sf9 cells: An importance of the N- Terminal domain for an allosteric regulatory property}},
volume = {159},
year = {2016}
}
@article{Seger2015,
abstract = {Main conclusion: The outcome of simultaneously increasing SPS and GS activities in transgenic tobacco, suggests that sucrose is the major determinant of growth and development, and is not affected by changes in N assimilation. Carbon (C) and nitrogen (N) are the major components required for plant growth and the metabolic pathways for C and N assimilation are very closely interlinked. Maintaining an appropriate balance or ratio of sugar to nitrogen metabolites in the cell, is important for the regulation of plant growth and development. To understand how C and N metabolism interact, we manipulated the expression of key genes in C and N metabolism individually and concurrently and checked for the repercussions. Transgenic tobacco plants with a cytosolic soybean glutamine synthetase (GS1) gene and a sucrose phosphate synthase (SPS) gene from maize, both driven by the CaMV 35S promoter were produced. Co-transformants, with both the transgenes were produced by sexual crosses. While GS is the key enzyme in N assimilation, involved in the synthesis of glutamine, SPS plays a key role in C metabolism by catalyzing the synthesis of sucrose. Moreover, to check if nitrate has any role in this interaction, the plants were grown under both low and high nitrogen. The SPS enzyme activity in the SPS and SPS/GS1 co-transformants were the same under both nitrogen regimens. However, the GS activity was lower in the co-transformants compared to the GS1 transformants, specifically under low nitrogen conditions. The GS1/SPS transformants showed a phenotype similar to the SPS transformants, suggesting that sucrose is the major determinant of growth and development in tobacco, and its effect is only marginally affected by increased N assimilation. Sucrose may be functioning in a metabolic capacity or as a signaling molecule.},
author = {Seger, Mark and Gebril, Sayed and Tabilona, Jules and Peel, Amanda and Sengupta-Gopalan, Champa},
doi = {10.1007/s00425-014-2165-4},
issn = {14322048},
journal = {Planta},
keywords = {C:N ratio,Co-transformants,Cytosolic glutamine synthetase (GS1),Sucrose phosphate synthase (SPS),Sucrose:starch ratio},
number = {1},
pages = {69--81},
pmid = {25213117},
title = {{Impact of concurrent overexpression of cytosolic glutamine synthetase (GS1) and sucrose phosphate synthase (SPS) on growth and development in transgenic tobacco}},
volume = {241},
year = {2015}
}
@article{Sonnewald1993,
abstract = {Sucrose-phosphate synthase (SPS) from leaves of spinach (Spinacia oleracea L.) has been purified to homogeneity by a procedure involving precipitation with polyethylenglycol and chromatography over diethylaminoethylcellulose, $\Omega$-aminohexylagarose, Mono Q and Blue Affinity columns. The purification factor was 838 and the final specific activity was 1.3 nkat {\textperiodcentered} (mg protein)-1. On denaturing gels the major polypeptide was 120 kDa but there was also a variable amount of smaller polypeptides in the range of 90 to 110 kDa. A new activity stain was developed to allow visualization of SPS in gels. The holoenzyme had a molecular weight of about 240 and 480 kDa in native gels and Sepharose, respectively. A high-titre polyclonal antibody was obtained which reacted with SPS from other species including wheat, potato, banana and maize. Screening of a spinach-leaf cDNA-expression library with the antibody allowed the isolation of a full-length clone. Sequencing revealed a predicted molecular weight of 117649 Da, and considerable homology with the recently published sequence for maize leaf (Worrell et al. 1991, Plant Cell 3, 1121-1130). Expression of the spinach-leaf SPS gene in Escherichia coli resulted in biological activity, revealed by the presence of SPS activity in extracts and the accumulation of sucrose-6-phosphate and sucrose in the bacteria. {\textcopyright} 1993 Springer-Verlag.},
author = {Sonnewald, U. and Quick, W. P. and MacRae, E. and Krause, K. P. and Stitt, Mark},
doi = {10.1007/BF00195074},
issn = {00320935},
journal = {Planta},
keywords = {Expression (spinach sucrose-phosphate synthase in,Nucleotide sequence (sucrosephosphate synthase),Spinacea,Sucrose-phosphate synthase (purification, cloning,,cDNA clone (encoding sucrose-phosphate synthase)},
number = {2},
pages = {174--181},
pmid = {7763376},
title = {{Purification, cloning and expression of spinach leaf sucrose-phosphate synthase in Escherichia coli}},
volume = {189},
year = {1993}
}
@article{Teck2008,
abstract = {Sucrose phosphate synthase (SPS) catalyzes the transfer of a glycosyl group from an activated donor sugar, such as uridine diphosphate glucose (UDP-Glc), to a saccharide acceptor D-fructose 6-phosphate (F6P), resulting in the formation of UDP and D-sucrose-6′-phosphate (S6P). This is a central regulatory process in the production of sucrose in plants, cyanobacteria, and proteobacteria. Here, we report the crystal structure of SPS from the nonphotosynthetic bacterium Halothermothrix orenii and its complexes with the substrate F6P and the product S6P. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate F6P and the product S6P bind to the A-domain of SPS. Based on comparative analysis of the SPS structure with other related enzymes, the donor substrate, nucleotide diphosphate glucose, binds to the B-domain of SPS. Furthermore, we propose a mechanism of catalysis by H. orenii SPS. Our findings indicate that SPS from H. orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme. {\textcopyright} 2008 American Society of Plant Biologists.},
author = {Teck, Khiang Chua and Bujnicki, Janusz M. and Tan, Tien Chye and Huynh, Frederick and Patel, Bharat K. and Sivaraman, J.},
doi = {10.1105/tpc.107.051193},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Teck et al. - 2008 - The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding.pdf:pdf;:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Teck et al. - 2008 - The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and bind(2).pdf:pdf},
issn = {10404651},
journal = {Plant Cell},
number = {4},
pages = {1059--1072},
pmid = {18424616},
title = {{The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode}},
volume = {20},
year = {2008}
}
@article{Toroser1999,
abstract = {Site-directed mutagenesis of spinach sucrose-phosphate synthase (SPS) was performed to investigate the role of Ser158 in the modulation of spinach leaf SPS. Tobacco plants expressing the spinach wild-type (WT), S158A, S158T and S157F/S158E SPS transgenes were produced. Expression of transgenes appeared not to reduce expression of the tobacco host SPS. SPS activity in the WT and the S158T SPS transgenics showed light/dark modulation, whereas the S158A and S157F/S158E mutants were not similarly light/dark modulated: the S158A mutant enzyme was not inactivated in the dark, and the S157F/S158E was not activated in the light. The inability to modulate the activity of the S158A mutant enzyme by protein phosphorylation was demonstrated in vitro. The WT spinach enzyme immunopurified from dark transgenic tobacco leaves had a low initial activation state, and could be activated by PP2A and subsequently inactivated by SPS-kinase plus ATP. Rapid purification of the S158A mutant enzyme from dark leaves of transgenic plants using spinach-specific monoclonal antibodies yielded enzyme that had a high initial activation state, and pre-incubation with leaf PP2A or ATP plus SPS-kinase (the PKIII enzyme) caused little modulation of activity. The results demonstrate the regulatory significance of Ser158 as the major site responsible for dark inactivation of spinach SPS in vivo, and indicate that the significance of phosphorylation is the introduction of a negative charge at the Ser158 position.},
author = {Toroser, Dikran and McMichael, Robert and Krause, Klause Peter and Kurreck, Jens and Sonnewald, Uwe and Stitt, Mark and Huber, Steven C.},
doi = {10.1046/j.1365-313X.1999.00389.x},
file = {:C\:/Users/hp/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Toroser et al. - 1999 - Site-directed mutagenesis of serine 158 demonstrates its role in spinach leaf sucrose-phosphate synthase modulat.pdf:pdf},
isbn = {0960-7412},
issn = {09607412},
journal = {Plant Journal},
number = {4},
pages = {407--413},
pmid = {10205897},
title = {{Site-directed mutagenesis of serine 158 demonstrates its role in spinach leaf sucrose-phosphate synthase modulation}},
volume = {17},
year = {1999}
}
@article{Worrell2016,
author = {Worrell, Ann C and Bruneau, Jean-michel and Summerfelt, Kristin and Boersig, Mike and Toni, A},
file = {:D\:/S2-Bioteknologi/thesis/jurnal manuscript/Worrell, 1991_Plant Cell.pdf:pdf},
number = {10},
pages = {1121--1130},
title = {{Expression of a Maize Sucrose Phosphate Synthase in Tomato Alters Leaf Carbohydrate Partitioning Published by : American Society of Plant Biologists ( ASPB ) Stable URL : http://www.jstor.org/stable/3869300 REFERENCES Linked references are available on JSTOR for this article : You may need to log in to JSTOR to access the linked references . Your use of the JSTOR archive indicates your acceptance of the Terms & Conditions of Use , available at http://www.jstor.org/page/ info / about / policies / terms . jsp JSTOR is a not-for-profit service that helps scholars , researchers , and students discover , use , and build upon a wide range of content in a trusted digital archive . We use information technology and tools to increase productivity and facilitate new forms of scholarship . For more information about JSTOR , please contact support@jstor.org . American Society of Plant Biologists ( ASPB ) is collaborating with JSTOR to digitize , preserve and extend access to The Plant All use subject to JSTOR Terms and Conditions All use subject to JSTOR Terms and Conditions}},
volume = {3},
year = {2016}
}