Dataset Information

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

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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]

PMID: 36981020

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Project description:In Arabidopsis thaliana the evolutionary conserved N-terminal acetyltransferase (Nat) complexes NatA and NatB co-translationally acetylate 60% of the proteome. Both have recently been implicated in the regulation of plant stress responses. While NatA mediates drought tolerance, NatB is required for pathogen resistance and the adaptation to high salinity and high osmolarity. Salt and osmotic stress impair protein folding and result in the accumulation of misfolded proteins in the endoplasmic reticulum (ER). The ER-membrane resident E3 ubiquitin ligase DOA10 targets misfolded proteins for degradation during ER stress and is conserved among eukaryotes. In yeast, DOA10 recognizes conditional degradation signals (Ac/N-degrons) created by NatA and NatB. Assuming that this mechanism is preserved in plants, the lack of Ac/N-degrons required for efficient removal of misfolded proteins might explain the sensitivity of NatB mutants to protein harming conditions. In this study, we investigate the response of NatB mutants to dithiothreitol (DTT) and tunicamycin (TM) induced ER stress. We report that NatB mutants are hypersensitive to DTT but not TM, suggesting that the DTT hypersensitivity is caused by an over-reduction of the cytosol rather than an accumulation of unfolded proteins in the ER. In line with this hypothesis, the cytosol of NatB depleted plants is constitutively over-reduced and a global transcriptome analysis reveals that their reductive stress response is permanently activated. Moreover, we demonstrate that doa10 mutants are susceptible to neither DTT nor TM, ruling out a substantial role of DOA10 in ER-associated protein degradation (ERAD) in plants. Contrary to previous findings in yeast, our data indicates that N-terminal acetylation (NTA) does not inhibit ER targeting of a substantial amount of proteins in plants. In summary, we provide further evidence that NatB-mediated imprinting of the proteome is vital for the response to protein-harming stress and rule out DOA10 as the sole recognin for substrates in the plant ERAD pathway.

Dataset Information

Proteomes and Ubiquitylome Analyses of Maize Endoplasmic Reticulum Under Heat Stress

Publications

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

Similar Datasets

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