Proteomics

Dataset Information

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Proteomes and Ubiquitylome Analyses of Maize Endoplasmic Reticulum Under Heat Stress


ABSTRACT: High temperature severely affects plant growth and threatens crop production. Heat causes accumulation of misfolded proteins in the ER and triggers heat shock response (HSR) in cytosol and unfolded protein response (UPR) in the ER. Excessive misfolded proteins further undergo degradation through ER associated degradation (ERAD). Although much work had been done on plant heat stress response, regulation of ER-localized proteins has not been well studied so far. We isolated the microsome fraction from heat treated and untreated maize seedlings and performed proteomics and ubtiquitylome analyses. 8306 proteins are detected by proteomics and 1675 and 708 proteins are significantly upregulated and downregulated respectively. Global ubiquitination analysis discovers 1780 proteins with at least one ubiquitination site in each protein. Motif analysis reveals that alanine and glycine are preferred at the upstream and downstream of the ubiquitinated lysine. ERAD components are found to be hyper-ubiquitinated after heat treatment, implying the feedback regulation of ERAD activity through protein degradation.

INSTRUMENT(S): LTQ Orbitrap, Orbitrap Fusion

ORGANISM(S): Zea Mays (maize)

TISSUE(S): Plant Cell, Shoot

DISEASE(S): Disease Free

SUBMITTER: chunyan Gao  

LAB HEAD: bensheng li

PROVIDER: PXD039418 | Pride | 2023-05-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
MS5992-TMT6plex-proteome.xlsx Xlsx
Ub-proteome_heat.xlsx Xlsx
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Publications

Proteome and Ubiquitylome Analyses of Maize Endoplasmic Reticulum under Heat Stress.

Gao Chunyan C   Peng Xiaohui X   Zhang Luoying L   Zhao Qi Q   Ma Liguo L   Yu Qi Q   Lian Xuechun X   Gao Lei L   Xiong Langyu L   Li Shengben S  

Genes 20230319 3


High temperatures severely affect plant growth and pose a threat to global crop production. Heat causes the accumulation of misfolded proteins in the endoplasmic reticulum(ER), as well as triggering the heat-shock response (HSR) in the cytosol and the unfolded protein response (UPR) in the ER. Excessive misfolded proteins undergo further degradation through ER-associated degradation (ERAD). Although much research on the plant heat stress response has been conducted, the regulation of ER-localize  ...[more]

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