Evidence map›Paper›PMID 36564499›Full record

ArticleFunctional & integrative genomics2022

Mechanistic insights into granule-bound starch synthase I (GBSSI.L539P) allele in high amylose starch biosynthesis in wheat (Triticum aestivum L.).

Vinita Sharma, Kousar Jahan, Prashant Kumar, Anuradhika Puri, Vishnu K Sharma, Ankita Mishra, P V Bharatam, Deepak Sharma, Vikas Rishi, Joy Roy

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Article in Functional & integrative genomics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 31% of its field
1 · What the graph read from it

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3 · Its place in the literature

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1 citing paper in PubMed, 8 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

10 authors at 5 institutions in 1 country.

Vinita SharmaNational Agri-Food Biotechnology Institute (NABI), SAS Nagar, Sector-81, Mohali, 140306, Punjab, India.
Kousar JahanDepartment of Medicinal Chemistry, National Institute of Pharmaceutical Education and Research (NIPER), SAS Nagar, Sector-67, Mohali, Punjab, 160062, India.
Prashant KumarNational Agri-Food Biotechnology Institute (NABI), SAS Nagar, Sector-81, Mohali, 140306, Punjab, India.
Anuradhika PuriInstitute of Microbial Technology, Council of Scientific and Industrial Research, Chandigarh, India.
Vishnu K SharmaDepartment of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research (NIPER), SAS Nagar, Sector-67, Mohali, Punjab, 160062, India.
Ankita MishraNational Agri-Food Biotechnology Institute (NABI), SAS Nagar, Sector-81, Mohali, 140306, Punjab, India.
P V BharatamDepartment of Medicinal Chemistry, National Institute of Pharmaceutical Education and Research (NIPER), SAS Nagar, Sector-67, Mohali, Punjab, 160062, India.
Deepak SharmaInstitute of Microbial Technology, Council of Scientific and Industrial Research, Chandigarh, India.
Vikas RishiNational Agri-Food Biotechnology Institute (NABI), SAS Nagar, Sector-81, Mohali, 140306, Punjab, India.
Joy RoyNational Agri-Food Biotechnology Institute (NABI), SAS Nagar, Sector-81, Mohali, 140306, Punjab, India. joykroy@nabi.res.in.
National Agri-Food Biotechnology Institute · INNational Institute of Pharmaceutical Education and Research · INCouncil of Scientific and Industrial Research · INIndian Institute of Science Education and Research Mohali · INInstitute of Microbial Technology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amylose fraction of grain starch is correlated with a type of resistant starch with better nutritional quality. Granule-bound starch synthase I (GBSSI) is the known starch synthase, responsible for elongation of linear amylose chains. GBSSI expression, activity, and binding to starch and other proteins are the key factors that can affect amylose content. Previously, a QTL, qhams7A.1 carrying GBSSI mutant allele, was identified through QTL mapping using F2 population of the high amylose mutant line, 'TAC 75'. This high amylose mutant line has >2-fold higher amylose content than wild variety 'C 306'. In this study, we characterized this novel mutant allele, GBSSI.L539P. In vitro starch synthase activity of GBSSI.L539P showed improved activity than the wild type (GBSSI-wt). When expressed in yeast glycogen synthase mutants (Δgsy1gsy2), GBSSI-wt and GBSSI.L539P partially complemented the glycogen synthase (gsy1gsy2) activity in yeast. Structural analysis by circular dichroism (CD) and homology modelling showed no significant structural distortion in the mutant enzyme. Molecular docking studies suggested that the residue Leu539 is distant from the catalytic active site (ADP binding pocket) and had no detectable conformational changes in active site. Both wild and mutant enzymes were assayed for starch binding in vitro, and demonstrating higher affinity of the GBSSI.L539P mutant for starch than the wild type. The present study indicated that distant residue (L539P) influenced GBSSI activity by affecting its starch-binding ability. Therefore, it may be a potential molecular target for enhanced amylose content in grain.

Indexed as

Starch SynthaseAllelesAmyloseGlycogen SynthaseMolecular Docking SimulationSaccharomyces cerevisiaeStarchTriticumAmyloseGlycogen Synthasegranule-bound starch synthase IStarchStarch SynthaseAmyloseBread wheatEnzyme activityGBSSIMolecular dockingStarch binding

Identifiers

PMID36564499
OpenAlexW4312117801

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.