Wheat genome specific granule-bound starch synthase I differentially influence grain starch synthesis

2014 ◽  
Vol 114 ◽  
pp. 87-94 ◽  
Author(s):  
Geetika Ahuja ◽  
Sarita Jaiswal ◽  
Pierre Hucl ◽  
Ravindra N. Chibbar
2012 ◽  
Vol 60 (40) ◽  
pp. 10082-10092 ◽  
Author(s):  
Eric K. Asare ◽  
Monica Båga ◽  
Brian G. Rossnagel ◽  
Ravindra N. Chibbar

2021 ◽  
Vol 12 ◽  
Author(s):  
Wenjing Zhang ◽  
Yan Zhao ◽  
Lingyu Li ◽  
Xu Xu ◽  
Li Yang ◽  
...  

Low temperatures (LT) in spring can have a major impact on the yields of wheat in winter. Wheat varieties with different cold sensitivities (the cold-tolerant Yannong 19 variety and the cold-sensitive Yangmai 18 variety) were used to study the responses of the wheat grain starch synthesis and dry material accumulation to short-term LT during the booting stage. The effects of short-term LT on the activities of key wheat grain starch synthesis enzymes, starch content and grain dry-matter accumulation were determined by exposing the wheat to simulated LT of from −2 to 2°C. Short-term LT stress caused a decrease in the fullness of the wheat grains along with decreased activities of adenosine diphosphate glucose pyrophosphorylase (AGPase, EC2.7.7.27), soluble starch synthase (SSS, EC2.4.1.21), granule-bound starch synthase (GBSS, EC2.4.1.21), and starch branching enzyme (SBE, EC2.4.1.18) at different spike positions during the filling stage. The rate of grain starch accumulation and starch content decreased with decreasing temperatures. Also, the duration of grain filling increased, the mean and the maximum filling rates were reduced and the quality of the grain dry-matter decreased. The number of grains per spike and the thousand-grain weight of the mature grains also decreased. Our data showed that short-term LT stress at the booting stage caused a decrease in the activities of key starch synthesis enzymes at the grain-filling stage. These changes reduced the accumulation of starch, decreased the filling rate, and lowered the accumulation of grain dry matter to ultimately decrease grain yields.


2006 ◽  
Vol 5 (6) ◽  
pp. 954-963 ◽  
Author(s):  
Philippe Deschamps ◽  
Ilka Haferkamp ◽  
David Dauvillée ◽  
Sophie Haebel ◽  
Martin Steup ◽  
...  

ABSTRACT The nature of the periplastidial pathway of starch biosynthesis was investigated with the model cryptophyte Guillardia theta. The storage polysaccharide granules were shown to be composed of both amylose and amylopectin fractions with a chain length distribution and crystalline organization very similar to those of starch from green algae and land plants. Most starch granules displayed a shape consistent with biosynthesis occurring around the pyrenoid through the rhodoplast membranes. A protein with significant similarity to the amylose-synthesizing granule-bound starch synthase 1 from green plants was found as the major polypeptide bound to the polysaccharide matrix. N-terminal sequencing of the mature protein proved that the precursor protein carries a nonfunctional transit peptide in its bipartite topogenic signal sequence which is cleaved without yielding transport of the enzyme across the two inner plastid membranes. The enzyme was shown to display similar affinities for ADP and UDP-glucose, while the V max measured with UDP-glucose was twofold higher. The granule-bound starch synthase from Guillardia theta was demonstrated to be responsible for the synthesis of long glucan chains and therefore to be the functional equivalent of the amylose-synthesizing enzyme of green plants. Preliminary characterization of the starch pathway suggests that Guillardia theta utilizes a UDP-glucose-based pathway to synthesize starch.


2009 ◽  
Vol 35 (2) ◽  
pp. 324-333 ◽  
Author(s):  
Peng-Fei CHU ◽  
Zhen-Wen YU ◽  
Xiao-Yan WANG ◽  
Tong-Hua WU ◽  
Xi-Zhi WANG

3 Biotech ◽  
2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Firoz Hossain ◽  
Rashmi Chhabra ◽  
Elangbam L. Devi ◽  
Rajkumar U. Zunjare ◽  
Sunil K. Jaiswal ◽  
...  

2012 ◽  
Vol 41 (Special Issue) ◽  
pp. 154-158
Author(s):  
J. Ovesná ◽  
M.-C. Nguyen ◽  
L. Kučera ◽  
V. Holubec

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