Unlike EC 2.4.1.11, glycogen(starch) synthase and EC 2.4.1.21, starch synthase, which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP- or ADP-glucose. Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose. In such mutants, only amylopectin is produced in the endosperm or pollen .
Unlike EC 2.4.1.11, glycogen(starch) synthase and EC 2.4.1.21, starch synthase, which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP- or ADP-glucose. Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose. In such mutants, only amylopectin is produced in the endosperm [3] or pollen [5].
enzyme is involved in the starch synthesis pathway synthesizing the amylose component, putative mechanism of regulation of GBSSI gene in photosynthetic tissue assuring the steady-state level of the isozyme, circadian oscillations of the mRNA level in leaves during day/night cycle, overview
enzyme is involved in the starch synthesis pathway synthesizing the amylose component, putative mechanism of regulation of GBSSI gene in photosynthetic tissue assuring the steady-state level of the isozyme, circadian oscillations of the mRNA level in leaves during day/night cycle, overview
protein targeting to starch, PTST, is required for localising granule-bound starch synthase to starch granules and for normal amylose synthesis. PTST is a plastidial protein possessing an N-terminal coiled coil domain and a C-terminal carbohydrate binding module. Enzyme GBSS physically interacts with protein PTST via a coiled coil. The CBM48 domain of PTST, which mediates its interaction with starch granules, is also required for correct GBSS localisation
protein targeting to starch, PTST, is required for localising granule-bound starch synthase to starch granules and for normal amylose synthesis. PTST is a plastidial protein possessing an N-terminal coiled coil domain and a C-terminal carbohydrate binding module, the CBM domain of PTST, which mediates its interaction with starch granules, is required for correct enzyme GBSS localisation. PTST remains in the stroma impliing that it interacts only transiently with starch during the GBSS localisation
protein targeting to starch, PTST, is required for localising granule-bound starch synthase to starch granules and for normal amylose synthesis. PTST is a plastidial protein possessing an N-terminal coiled coil domain and a C-terminal carbohydrate binding module, the CBM domain of PTST, which mediates its interaction with starch granules, is required for correct enzyme GBSS localisation. PTST remains in the stroma impliing that it interacts only transiently with starch during the GBSS localisation
Arabidopsis thaliana mutants lacking plastidial protein PTST synthesise amylose-free starch and are phenotypically similar to mutants lacking granule-bound starch synthase GBSS. PTST mutant starch granules show a dramatic reduction of GBSS protein. GBSS physically interacts with PTST via a coiled coil. The carbohydrate binding module of PTST, which mediates its interaction with starch granules, is also required for correct GBSS localisation. Arabidopsis GBSS requires the presence of Arabidopsis PTST to localise to starch granules. Mutation of the carbohydrate binding module of PTST causes GBSS to remain in the plastid stroma
Arabidopsis thaliana ptst mutants synthesise amylose-free starch and are phenotypically similar to mutants lacking GBSS. Mutation of the CBM domain of PTST causes GBSS to remain in the plastid stroma
GBSS1 is the key enzyme in amylose synthesis and exclusively controls all enzyme activities in this pathway, overview. GBSS1 activity is increased compared to wild-type when soluble starch synthases SS2 and SS1 are missing, and the total amount of amylose in the leaves is elevated, SS1 and SS2 activity both can influence the activity of GBSS1
construction of transgenic plants overexpressing the transcription factor CCA1 that show an altered circadian rhythm, overexpression of both transcription factor CCA1 and LHY causes elimination of mRNA level oscillation
construction of diverse soluble starch synthases ss mutants, with or without mutation of GBSS1, e.g. gbss1- ss2-double mutant and gbss1- ss1- ss2-triple mutant, waxy gene, phenotypes, overview
recombinant expression of C-terminally HA and cyan fluorescent protein (CFP) tandem tagged wild-type nd mutant enzymes in Arabidopsis thaliana leaves via Agrobactrium tumefaciens transformation and in Nicotiana tabacum epidermal cells. Wild-type GBSS enzyme is only detected in the immunoprecipitate when TAP-tagged PTST is coexpressed, confirming the protein-protein interaction
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcript encoding granule-bound starch synthase GBSS1 accumulates to a higher level in carbon catabolite repressor CCR4a/CCR4b double mutant plants than in the control plants. GBSS1 has a longer poly(A) tail in the double mutant than in the control plant, suggesting that CCR4a and CCR4b can influence the poly(A) length of transcripts related to starch metabolism
Suzuki, Y.; Arae, T.; Green, P.J.; Yamaguchi, J.; Chiba, Y.
AtCCR4a and AtCCR4b are involved in determining the poly(A) length of granule-bound starch synthase 1 transcript and modulating sucrose and starch metabolism in Arabidopsis thaliana
PROTEIN TARGETING TO STARCH is required for localising GRANULE-BOUND STARCH SYNTHASE to starch granules and for normal amylose synthesis in Arabidopsis