scholarly journals Starch Synthesis in Ostreococcus tauri: The Starch-Binding Domains of Starch Synthase III-B Are Essential for Catalytic Activity

2018 ◽  
Vol 9 ◽  
Author(s):  
Julieta Barchiesi ◽  
Maria Belen Velazquez ◽  
Nicolas Palopoli ◽  
Alberto A. Iglesias ◽  
Diego F. Gomez-Casati ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Starch Synthesis ◽  
Starch Synthase ◽  
Ostreococcus Tauri ◽  
Binding Domains

Effect of high temperature during grain filling on starch synthesis in the developing barley grain

1998 ◽  
Vol 25 (2) ◽  
pp. 173 ◽  
Author(s):  
M. A. B. Wallwork ◽  
S. J. Logue ◽  
L. C. MacLeod ◽  
C. F. Jenner
Keyword(s):  
Catalytic Activity ◽  
High Temperature ◽  
High Temperatures ◽  
Starch Synthesis ◽  
Grain Filling ◽  
Soluble Starch ◽  
Barley Grain ◽  
Starch Synthase ◽  
Heat Treated ◽  
C 30

Plants of malting barley variety Schooner were exposed to 5 days of high temperatures (up to 35°C) during mid grain filling under controlled environment conditions. Grains from heat treated plants accumulated c. 30% less starch than grains from control plants (21/16°C; 14 h day). Reduced starch deposition was not limited by assimilate levels in heat treated grains, but high temperature reduced the conversion of sucrose to starch. The reduction in starch synthesis appeared to result from the effects of diminished catalytic activity of a number of enzymes in the committed pathway of starch synthesis, and/or delayed recovery of enzyme activity in the cooler recovery conditions. Reductions of 11–75% in the activity of the enzymes under investigation followed high temperature exposure. In addition, ADPglucose pyrophosphorylase, branching enzyme and granule bound starch synthase showed increased activity during exposure to moderate temperatures (28–32°C), but reduced activity at high temperatures, while soluble starch synthase showed an immediate loss of activity, even at moderate temperatures. Sucrose synthase and UDPglucose pyrophosphorylase showed the greatest reduction in catalytic activity after plants were returned to cooler conditions. Individual enzymes showed variation in the level of recovery under the cooler temperature conditions which followed the heating period.

scholarly journals Triple null mutations in starch synthase SSIIa gene homoeologs lead to high amylose and resistant starch in hexaploid wheat

2020 ◽  
Author(s):  
Adam Schoen ◽  
Anupama Joshi ◽  
Vijay K Tiwari ◽  
Bikram S. Gill ◽  
Nidhi Rawat
Keyword(s):  
Resistant Starch ◽  
Amylose Content ◽  
Starch Content ◽  
Wheat Variety ◽  
Starch Synthesis ◽  
Starch Synthase ◽  
Single Individual ◽  
Individual Genome ◽  
Mutant Genotype ◽  
Knock Out

Abstract Background: Lack of nutritionally appropriate foods is one of the leading causes of obesity in the US and worldwide. Wheat (Triticum aestivum) provides 20% of the calories consumed daily across the globe. The nutrients in the wheat grain come primarily from the starch composed of amylose and amylopectin. Resistant starch content, which is known to have significant human health benefits, can be increased by modifying starch synthesis pathways. Starch synthase enzyme SSIIa, also known as starch granule protein isoform-1 (SGP-1), is integral to the biosynthesis of the branched and readily digestible glucose polymer amylopectin. The goal of this work was to develop a triple null mutant genotype for SSIIa locus in the elite hard red winter wheat variety ‘Jagger’ and evaluate the effect of the knock-out mutations on resistant starch content in grains with respect to wild type. Results: Knock-out mutations in SSIIa in the three genomes of wheat variety ‘Jagger’ were identified using TILLING. Subsequently, these loss-of function mutations on A, B, and D genomes were combined by crossing to generate a triple knockout mutant genotype Jag-ssiia-∆ABD. The Jag-ssiia-∆ABD had an amylose content of 35.70% compared to 31.15% in Jagger, leading to ~118% increase in resistant starch in the Jag-ssiia-∆ABD genotype of Jagger wheat. The single individual genome mutations also had various effects on starch composition. Conclusions: Our full null Jag-ssiia-∆ABD mutant showed a significant increase in RS without the shriveled grain phenotype seen in other ssiia knockouts in elite wheat cultivars. Moreover, this study shows the potential for developing nutritionally improved foods in a non-GM approach. Since all the mutants have been developed in an elite wheat cultivar, their adoption in production and supply will be feasible in future.

Effects of Elevated Temperature and Reduced Water Uptake on Enzymes of Starch Synthesis in Developing Wheat Grains

1990 ◽  
Vol 17 (4) ◽  
pp. 431 ◽  
Author(s):  
CY Caley ◽  
CM Duffus ◽  
B Jeffcoat
Keyword(s):  
Elevated Temperatures ◽  
Starch Content ◽  
Starch Synthesis ◽  
Dry Weight ◽  
Endosperm Development ◽  
Starch Synthase ◽  
Temperature Regimes ◽  
Endosperm Starch ◽  
Rate Limiting ◽  
Reduced Water

The mechanism of temperature regulation of endosperm development has been investigated by studying the effects of two temperature regimes on starch deposition and starch synthase activity during grain development in two cultivars of wheat. Most of the starch synthase activity was present throughout development as the granule-bound form using ADPglucose as the principal substrate. That starch synthase may be a rate-limiting enzyme for accumulation of starch, and hence dry weight, is suggested by: (1) rates are proportionately less in the cultivar with the lower final endosperm dry weight; (2) at elevated temperatures when starch content and dry weight are reduced, starch synthase activity falls; (3) the rate of starch deposition calculated to be possible from measured rates of starch synthase activity is close to the observed rate of starch deposition. On the other hand, it was concluded that it is not lack of starch synthase activity that causes termination of starch deposition, since activity is maintained well after starch deposition has ceased. Using the same two wheat cultivars, grown as detached ears in liquid culture, the effects of reduced endosperm water content, induced by the presence of polyethylene glycol in the culture medium, were investigated. Endosperm starch synthase activity was unaffected but ADPglucose pyrophosphorylase activity was greatly reduced, suggesting a possible role in the termination of starch synthesis.

The targeting of starch binding domains from starch synthase III to the cell wall alters cell wall composition and properties

2016 ◽  
Vol 93 (1-2) ◽  
pp. 121-135 ◽  
Author(s):  
Mauricio J. Grisolia ◽  
Diego A. Peralta ◽  
Hugo A. Valdez ◽  
Julieta Barchiesi ◽  
Diego F. Gomez-Casati ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Wall Composition ◽  
Starch Synthase ◽  
Binding Domains

Salt Tolerance and Regulation of Enzymes of Starch Synthesis in Cassava (Manihot esculenta Crantz)

1982 ◽  
Vol 9 (5) ◽  
pp. 509 ◽  
Author(s):  
JS Hawker ◽  
GM Smith
Keyword(s):  
Manihot Esculenta ◽  
Starch Synthesis ◽  
Starch Synthase ◽  
Manihot Esculenta Crantz ◽  
Adpglucose Pyrophosphorylase ◽  
Storage Organs ◽  
Porous Growth ◽  
Phosphoglyceric Acid ◽  
And Storage ◽  
Nutrient Solutions

The growth rate of cassava plants (Manihot esculenta cv. MAUS7) decreased with increasing concentrations of NaCl from 0 to 75 mM in nutrient solutions supplied regularly in a porous growth medium in a glasshouse. Tuber weight was reduced to one-half between 30 and 50 mM NaCl and there was some burning of apical leaves at 50 and 75 mM NaCl. By comparison with other plants, this cultivar of cassava can be considered to have medium sensitivity to salinity. Na+ and Cl- concentrations increased in all tissues with increasing concentrations of supplied NaCl, except that Na+ remained low in laminae until the 75 mM treatment. K+ levels decreased in tubers. Starch concentrations remained the same in tubers, and K+ stimulated starch bound ADPglucose starch synthase by 1 .5-fold. Leaves and tubers contained activities of ADPglucose pyrophosphorylase and ADPglucose-starch synthase similar to those found in leaves and storage organs of other starch synthesizing plants. ADPglucose pyrophosphorylase from leaves was stimulated 20-fold by 3-phosphoglyceric acid (3PGA) while the enzyme from tubers was almost completely dependent on 3PGA at pH 8.5. The A0.5 values for 3PGA (the concentration required for one-half maximal activation) for the leaf and tuber enzymes at pH 8.5 were 1.31 mM and 7.41 mM respectively. At pH 7.5 the leaf enzyme was stimulated 26-fold and the tuber enzyme was again almost completely dependent on 3PGA. The A0.5 values at pH 7.5 were 1.17 mM and 3.8 mM, respectively. The I0.5 values for PI (concentrations required to cause 50% inhibition) in the presence of 3PGA were 2 mM, 0.25 mM and 0.04 mM for leaf enzyme at pH 8.5 and tuber enzyme at pH 8.5 and 7.7 respectively. The results support the view that it is not possible to generalize about the magnitude of the control of ADPglucose synthesis in leaves as opposed to non-chlorophyllous tissues.

scholarly journals Interplay Between the N-Terminal Domains of Arabidopsis Starch Synthase 3 Determines the Interaction of the Enzyme With the Starch Granule

2021 ◽  
Vol 12 ◽  
Author(s):  
Francisco M. Gámez-Arjona ◽  
Ángel Mérida
Keyword(s):  
Starch Granule ◽  
Coiled Coil ◽  
Terminal Region ◽  
Starch Synthase ◽  
Full Length ◽  
Localization Pattern ◽  
Binding Domains ◽  
Starch Synthases ◽  
Linear Chains

The elongation of the linear chains of starch is undertaken by starch synthases. class 3 of starch synthase (SS3) has a specific feature: a long N-terminal region containing starch binding domains (SBDs). In this work, we analyze in vivo the contribution of these domains to the localization pattern of the enzyme. For this purpose, we divided the N-terminal region of Arabidopsis SS3 in three domains: D1, D2, and D3 (each of which contains an SBD and a coiled-coil site). Our analyses indicate that the N-terminal region is sufficient to determine the same localization pattern observed with the full-length protein. D2 binds tightly the polypeptide to the polymer and it is necessary the contribution of D1 and D3 to avoid the polypeptide to be trapped in the growing polymer. The localization pattern of Arabidopsis SS3 appears to be the result of the counterbalanced action of the different domains present in its N-terminal region.

scholarly journals Structure & acceptor recognition of CLG1_GBSS, a cyanobacterial starch synthase.

2014 ◽  
Vol 70 (a1) ◽  
pp. C1167-C1167
Author(s):  
Jose Cuesta-Seijo ◽  
Morten Nielsen ◽  
Monica Palcic
Keyword(s):  
Starch Granule ◽  
Glycogen Synthase ◽  
Starch Synthesis ◽  
Caloric Intake ◽  
Starch Synthase ◽  
Complex Structures ◽  
Asymmetric Unit ◽  
Group V ◽  
The World ◽  
Shed Light

Starch synthesis was thought to occur exclusively in archaeplastida, which include green algae and land plants. Recently, amylopectin-like polymers have been identified in group V cyanobacteria[1]. In particular, a newly isolated cyanobacterium, CLG1, synthetizes granules containing both amylose and amylopectin essentially identical to plant starch[2]. These cyanobacteria are believed to have contributed some of the key starch synthesizing enzymes to plants. Starch synthases are the enzymes responsible for elongation of the maltooligosaccharide chains that compose the starch granule, working in concert with many other enzymes to create the complex structures of amylopectin and amylose. Here we report the crystal structure, refined to 2.2 Å, of GBSS, the granule bound starch synthase responsible for amylose synthesis in CLG1, in complex with ADP and either acarbose or glucose in the acceptor binding site. The structure reveals different conformational states of the ternary complex in three copies of GBSS in the asymmetric unit. The variations between monomers shed light on changes on the protein upon substrate recognition. In particular it clarifies the effect of acceptor binding in the conformation of the active site. This structure also illustrates the conformation of parts of the primary sequence that were absent from all plant starch synthase structures to date. Features in this structure are compared to both glycogen synthase and starch synthase structures. Both the similarities and the differences advance our knowledge on the necessary components of a starch synthase and point the way to their targeted structural and functional modification. The world-wide demand of cereals is expected to double from its current values by 2050 (FAO). Modification of proteins involved in starch synthesis, be it via traditional breeding or via genetic engineering, will likely be crucial to meeting the caloric intake needs of the human population in the coming decades.

scholarly journals Triple null mutations in starch synthase SSIIa gene homoeologs lead to high amylose and resistant starch in hexaploid wheat

2021 ◽  
Author(s):  
Adam Schoen ◽  
Anupama Joshi ◽  
Vijay K Tiwari ◽  
Bikram S. Gill ◽  
Nidhi Rawat
Keyword(s):  
Resistant Starch ◽  
Amylose Content ◽  
Starch Content ◽  
Wheat Variety ◽  
Starch Synthesis ◽  
Starch Synthase ◽  
Single Individual ◽  
Individual Genome ◽  
Mutant Genotype ◽  
Knock Out

Abstract Background: Lack of nutritionally appropriate foods is one of the leading causes of obesity in the US and worldwide. Wheat (Triticum aestivum) provides 20% of the calories consumed daily across the globe. The nutrients in the wheat grain come primarily from the starch composed of amylose and amylopectin. Resistant starch content, which is known to have significant human health benefits, can be increased by modifying starch synthesis pathways. Starch synthase enzyme SSIIa, also known as starch granule protein isoform-1 (SGP-1), is integral to the biosynthesis of the branched and readily digestible glucose polymer amylopectin. The goal of this work was to develop a triple null mutant genotype for SSIIa locus in the elite hard red winter wheat variety ‘Jagger’ and evaluate the effect of the knock-out mutations on resistant starch content in grains with respect to wild type. Results: Knock-out mutations in SSIIa in the three genomes of wheat variety ‘Jagger’ were identified using TILLING. Subsequently, these loss-of function mutations on A, B, and D genomes were combined by crossing to generate a triple knockout mutant genotype Jag-ssiia-∆ABD. The Jag-ssiia-∆ABD had an amylose content of 35.70% compared to 31.15% in Jagger, leading to ~118% increase in resistant starch in the Jag-ssiia-∆ABD genotype of Jagger wheat. The single individual genome mutations also had various effects on starch composition. Conclusions: Our full null Jag-ssiia-∆ABD mutant showed a significant increase in RS without the shriveled grain phenotype seen in other ssiia knockouts in elite wheat cultivars. Moreover, this study shows the potential for developing nutritionally improved foods in a non-GM approach. Since all the mutants have been developed in an elite wheat cultivar, their adoption in production and supply will be feasible in future.

Sign in / Sign up

Export Citation Format

Share Document