In vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response
Abstract Background Drought stress during grain development causes significant yield loss in cereal production. The phosphorylated modification of starch granule-binding proteins (SGBPs) is an important mechanism regulating wheat starch biosynthesis. In this study, we performed the first proteomics...
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doaj-d27b9652562046c3afe619c55a94cab62020-11-25T02:32:25ZengBMCBMC Plant Biology1471-22292017-10-0117111310.1186/s12870-017-1118-zIn vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit responseGuan-Xing Chen0Shou-Min Zhen1Yan-Lin Liu2Xing Yan3Ming Zhang4Yue-Ming Yan5College of Life Science, Capital Normal UniversityCollege of Life Science, Capital Normal UniversityCollege of Life Science, Capital Normal UniversityCollege of Life Science, Capital Normal UniversityCollege of Life Science, Capital Normal UniversityCollege of Life Science, Capital Normal UniversityAbstract Background Drought stress during grain development causes significant yield loss in cereal production. The phosphorylated modification of starch granule-binding proteins (SGBPs) is an important mechanism regulating wheat starch biosynthesis. In this study, we performed the first proteomics and phosphoproteomics analyses of SGBPs in elite Chinese bread wheat (Triticum aestivum L.) cultivar Jingdong 17 under well-watered and water-stress conditions. Results Water stress treatment caused significant reductions in spike grain numbers and weight, total starch and amylopectin content, and grain yield. Two-dimensional gel electrophoresis revealed that the quantity of SGBPs was reduced significantly by water-deficit treatment. Phosphoproteome characterization of SGBPs under water-deficit treatment demonstrated a reduced level of phosphorylation of main starch synthesis enzymes, particularly for granule-bound starch synthase (GBSS I), starch synthase II-a (SS II-a), and starch synthase III (SS III). Specifically, the Ser34 site of the GBSSI protein, the Tyr358 site of SS II-a, and the Ser837 site of SS III-a exhibited significant less phosphorylation under water-deficit treatment than well-watered treatment. Furthermore, the expression levels of several key genes related with starch biosynthesis detected by qRT-PCR were decreased significantly at 15 days post-anthesis under water-deficit treatment. Immunolocalization showed a clear movement of GBSS I from the periphery to the interior of starch granules during grain development, under both water-deficit and well-watered conditions. Conclusions Our results demonstrated that the reduction in gene expression or transcription level, protein expression and phosphorylation levels of starch biosynthesis related enzymes under water-deficit conditions is responsible for the significant decrease in total starch content and grain yield.http://link.springer.com/article/10.1186/s12870-017-1118-zTriticum aestivum L.Water-deficitStarch granule-binding proteinsPhosphoproteomeBioinformatics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Guan-Xing Chen Shou-Min Zhen Yan-Lin Liu Xing Yan Ming Zhang Yue-Ming Yan |
spellingShingle |
Guan-Xing Chen Shou-Min Zhen Yan-Lin Liu Xing Yan Ming Zhang Yue-Ming Yan In vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response BMC Plant Biology Triticum aestivum L. Water-deficit Starch granule-binding proteins Phosphoproteome Bioinformatics |
author_facet |
Guan-Xing Chen Shou-Min Zhen Yan-Lin Liu Xing Yan Ming Zhang Yue-Ming Yan |
author_sort |
Guan-Xing Chen |
title |
In vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response |
title_short |
In vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response |
title_full |
In vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response |
title_fullStr |
In vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response |
title_full_unstemmed |
In vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response |
title_sort |
in vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response |
publisher |
BMC |
series |
BMC Plant Biology |
issn |
1471-2229 |
publishDate |
2017-10-01 |
description |
Abstract Background Drought stress during grain development causes significant yield loss in cereal production. The phosphorylated modification of starch granule-binding proteins (SGBPs) is an important mechanism regulating wheat starch biosynthesis. In this study, we performed the first proteomics and phosphoproteomics analyses of SGBPs in elite Chinese bread wheat (Triticum aestivum L.) cultivar Jingdong 17 under well-watered and water-stress conditions. Results Water stress treatment caused significant reductions in spike grain numbers and weight, total starch and amylopectin content, and grain yield. Two-dimensional gel electrophoresis revealed that the quantity of SGBPs was reduced significantly by water-deficit treatment. Phosphoproteome characterization of SGBPs under water-deficit treatment demonstrated a reduced level of phosphorylation of main starch synthesis enzymes, particularly for granule-bound starch synthase (GBSS I), starch synthase II-a (SS II-a), and starch synthase III (SS III). Specifically, the Ser34 site of the GBSSI protein, the Tyr358 site of SS II-a, and the Ser837 site of SS III-a exhibited significant less phosphorylation under water-deficit treatment than well-watered treatment. Furthermore, the expression levels of several key genes related with starch biosynthesis detected by qRT-PCR were decreased significantly at 15 days post-anthesis under water-deficit treatment. Immunolocalization showed a clear movement of GBSS I from the periphery to the interior of starch granules during grain development, under both water-deficit and well-watered conditions. Conclusions Our results demonstrated that the reduction in gene expression or transcription level, protein expression and phosphorylation levels of starch biosynthesis related enzymes under water-deficit conditions is responsible for the significant decrease in total starch content and grain yield. |
topic |
Triticum aestivum L. Water-deficit Starch granule-binding proteins Phosphoproteome Bioinformatics |
url |
http://link.springer.com/article/10.1186/s12870-017-1118-z |
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