scholarly journals PROTEIN TARGETING TO STARCH Is Required for Localising GRANULE-BOUND STARCH SYNTHASE to Starch Granules and for Normal Amylose Synthesis in Arabidopsis

PLoS Biology ◽  
2015 ◽  
Vol 13 (2) ◽  
pp. e1002080 ◽  
Author(s):  
David Seung ◽  
Sebastian Soyk ◽  
Mario Coiro ◽  
Benjamin A. Maier ◽  
Simona Eicke ◽  
...  
Keyword(s):  
Protein Targeting ◽  
Starch Synthase ◽  
Starch Granules ◽  
Granule Bound Starch Synthase

scholarly journals Granule-bound starch synthase I in isolated starch granules elongates malto-oligosaccharides processively

1999 ◽  
Vol 340 (1) ◽  
pp. 183-191 ◽  
Author(s):  
Kay DENYER ◽  
Darren WAITE ◽  
Saddik MOTAWIA ◽  
Birger Lindberg MØLLER ◽  
Alison M. SMITH
Keyword(s):  
Starch Synthase ◽  
Kinetic Properties ◽  
Starch Granules ◽  
Wild Type ◽  
Lower Affinity ◽  
Functional Differences ◽  
Glucose Molecule ◽  
Granule Bound Starch Synthase

Isoforms of starch synthase belonging to the granule-bound starch synthase I (GBSSI) class synthesize the amylose component of starch in plants. Other granule-bound isoforms of starch synthase, such as starch synthase II (SSII), are unable to synthesize amylose. The kinetic properties of GBSSI and SSII that are responsible for these functional differences have been investigated using starch granules from embryos of wild-type peas and rug5 and lam mutant peas, which contain, respectively, both GBSSI and SSII, GBSSI but not SSII and SSII but not GBSSI. We show that GBSSI in isolated granules elongates malto-oligosaccharides processively, adding more than one glucose molecule for each enzyme-glucan encounter. Granule-bound SSII can elongate malto-oligosaccharides, but has a lower affinity for these than GBSSI and does not elongate processively. As a result of these properties GBSSI synthesizes longer malto-oligosaccharides than SSII. The significance of these results with respect to the roles of GBSSI and SSII in vivo is discussed.

scholarly journals Purification of Starch Granules from Arabidopsis Leaves and Determination of Granule-Bound Starch Synthase Activity

BIO-PROTOCOL ◽  
2014 ◽  
Vol 4 (23) ◽  
Author(s):  
Tomás Albi ◽  
M. Ortiz-Marchena ◽  
M. Ruiz ◽  
José Romero ◽  
Federico Valverde
Keyword(s):  
Starch Synthase ◽  
Starch Granules ◽  
Granule Bound Starch Synthase

scholarly journals Granule-bound starch synthase I in isolated starch granules elongates malto-oligosaccharides processively

1999 ◽  
Vol 340 (1) ◽  
pp. 183 ◽  
Author(s):  
Kay DENYER ◽  
Darren WAITE ◽  
Saddik MOTAWIA ◽  
Birger Lindberg MØLLER ◽  
Alison M. SMITH
Keyword(s):  
Starch Synthase ◽  
Starch Granules ◽  
Granule Bound Starch Synthase

scholarly journals Protein Targeting to Starch Synthase 1, a Functional Protein of Starch Biosynthesis in Wheat (Triticum Aestivum L.)

2021 ◽  
Author(s):  
Vinita Sharma ◽  
Vikas Fandade ◽  
Prashant Kumar ◽  
Afsana Parveen ◽  
Akansha Madhawan ◽  
...  
Keyword(s):  
Protein Targeting ◽  
Homology Modelling ◽  
Wheat Variety ◽  
Coiled Coil ◽  
Starch Synthase ◽  
Bimolecular Fluorescence Complementation ◽  
Starch Granules ◽  
Wheat Endosperm ◽  
Native Starch ◽  
Coiled Coil Domain

Abstract In cereal endosperm, native starch comprising amylose and amylopectin is synthesized by the coordinated activities of several pathway enzymes. Amylose in starch influences its physio-chemical properties resulting in several human health benefits. The Granule-Bound Starch Synthase I (GBSSI) is the most abundant starch-associated protein. GBSSI lacks dedicated Carbohydrate-binding module (CBM). Previously, Protein Targeting Starch Synthase 1 (PTST1) was identified as a crucial protein for the localization of GBSSI to the starch granules in Arabidopsis. The function of its homologous protein in the wheat endosperm is not known. In this study, TaPTST1, an AtPTST1 homolog, containing a CBM and a coiled-coil domain was identified in wheat. Protein-coding nucleotide sequence of TaPTST1 from Indian wheat variety ‘C 306’ was cloned and characterized. Homology modelling and molecular docking suggested the potential interaction of TaPTST1 with glucans and GBSSI. The TaPTST1 expression was higher in wheat grain than the other tissues, suggesting a grain-specific function. In vitro binding assays demonstrated different binding affinities of TaPTST1 for native starch, amylose, and amylopectin. Furthermore, the immunoaffinity pull-down assay revealed that TaPTST1 directly interacts with GBSSI, and the interaction is mediated by a coiled-coil domain. The direct protein-protein interaction was further confirmed by bimolecular fluorescence complementation assay (BiFC) in planta. Based on our findings we postulate a functional role for TaPTST1 in starch metabolism by targeting GBSSI to starch granules in wheat endosperm.

scholarly journals Molecular analysis of mutant granule-bound starch synthase-I (waxy1) gene in diverse waxy maize inbreds

3 Biotech ◽  
2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Firoz Hossain ◽  
Rashmi Chhabra ◽  
Elangbam L. Devi ◽  
Rajkumar U. Zunjare ◽  
Sunil K. Jaiswal ◽  
...  
Keyword(s):  
Molecular Analysis ◽  
Starch Synthase ◽  
Waxy Maize ◽  
Maize Inbreds ◽  
Granule Bound Starch Synthase

scholarly journals Diversity of granule bound starch synthase i coding sequence within selected wild and cultivated Triticeae

2012 ◽  
Vol 41 (Special Issue) ◽  
pp. 154-158
Author(s):  
J. Ovesná ◽  
M.-C. Nguyen ◽  
L. Kučera ◽  
V. Holubec
Keyword(s):  
Full Text ◽  
Starch Synthase ◽  
Coding Sequence ◽  
Granule Bound Starch Synthase

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