PXD002805

PXD002805 is an original dataset announced via ProteomeXchange.

Title	New Insights into the Biosynthesis and Regulation of Wheat Amylose and Amylopectin from Proteomic and Phosphoproteomic Characterization of Granule-binding Proteins
Description	Waxy starch has an important influence on bread dough and the qualities of breads. Generally, grain weight and yield in waxy wheat (Triticum aestivum L.) are significantly lower than in bread wheat. In this study, we performed the first proteomic and phosphoproteomic analyses of starch granule-binding proteins by comparing the waxy wheat cultivar Shannong 119 and the bread wheat cultivar Nongda 5181. The waxy and non-waxy wheats had similar starch granule morphological features and developmental patterns, and similar amylopectin quality in the grain. These results indicate that reduced amylose content does not affect amylopectin synthesis, but it causes significant reduction of total starch biosynthesis, grain size, weight and yield. Two-dimensional differential in-gel electrophoresis identified 40 differentially expressed protein (DEP) spots in waxy and non-waxy wheats, which belonged mainly to starch synthase (SS) I, SS IIa and granule-bound SS I. Most DEPs involved in amylopectin synthesis showed a similar expression pattern during grain development, suggesting relatively independent amylose and amylopectin synthesis pathways. Phosphoproteome analysis of starch granule-binding proteins, using TiO2 microcolumns and LC-MS/MS, showed that the total number of phosphoproteins and their phosphorylation levels in ND5181 were significantly higher than in SN119, but proteins controlling amylopectin synthesis had similar phosphorylation levels. Dynamic transcriptional expression profiling of starch biosynthesis-related genes indicated similar transcriptional expression profiles in both cultivars. Our results revealed that phosphorylation modifications played critical roles in amylose and amylopectin biosynthesis, but the lack of amylose did not affect the expression and phosphorylation of the starch granule-binding proteins involved in amylopectin biosynthesis.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:25:55.052.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Guanxing Chen
SpeciesList	scientific name: Triticum aestivum (Wheat); NCBI TaxID: 4565;
ModificationList	phosphorylated residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2015-08-27 02:41:51	ID requested
1	2017-10-30 03:15:46	announced
⏵ 2	2024-10-22 04:26:03	announced	2024-10-22: Updated project metadata.

10.1186/s12870-017-1118-z;

Chen GX, Zhen SM, Liu YL, Yan X, Zhang M, Yan YM, In vivo phosphoproteome characterization reveals key starch granule-binding phosphoproteins involved in wheat water-deficit response. BMC Plant Biol, 17(1):168(2017) [pubmed]

curator keyword: Biological

submitter keyword: Proteomic,Granule-binding Proteins,Phosphoproteomic

Yue-Ming Yan
contact affiliation	College of Life Science, Capital Normal University, 100048 Beijing, China
contact email	yanym@cnu.edu.cn
lab head
Guanxing Chen
contact affiliation	nercv
contact email	chenguanxing@nercv.org
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002805
     1. Label: PRIDE project
     2. Name: New Insights into the Biosynthesis and Regulation of Wheat Amylose and Amylopectin from Proteomic and Phosphoproteomic Characterization of Granule-binding Proteins