2. Academic Validation
  3. Proteome and Ubiquitylome Analyses of Maize Endoplasmic Reticulum under Heat Stress

Proteome and Ubiquitylome Analyses of Maize Endoplasmic Reticulum under Heat Stress

  • Genes (Basel). 2023 Mar 19;14(3):749. doi: 10.3390/genes14030749.
Chunyan Gao 1 2,  Xiaohui Peng 1,  Luoying Zhang 1,  Qi Zhao 1,  Liguo Ma 1,  Qi Yu 1,  Xuechun Lian 1,  Lei Gao 3 4,  Langyu Xiong 5,  Shengben Li 1 6
Affiliations

Affiliations

  • 1 State Key Laboratory of Crop Genetics & Germplasm Enhancement and Utilization, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China.
  • 2 College of Agriculture, Nanjing Agricultural University, Nanjing 210095, China.
  • 3 College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China.
  • 4 Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China.
  • 5 Institute of Advanced Studies in Humanities and Social Sciences, Beijing Normal University, Zhuhai 519087, China.
  • 6 Academy for Advanced Interdisciplinary Studies, Nanjing Agricultural University, Nanjing 210095, China.
PMID: 36981020 DOI: 10.3390/genes14030749
Abstract

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-localized proteins has not been well-studied thus far. We isolated the microsome fraction from heat-treated and untreated maize seedlings and performed proteome and ubiquitylome analyses. Of the 8306 total proteins detected in the proteomics analysis, 1675 proteins were significantly up-regulated and 708 proteins were significantly down-regulated. Global ubiquitination analysis revealed 1780 proteins with at least one ubiquitination site. Motif analysis revealed that alanine and glycine are the preferred Amino acids upstream and downstream of ubiquitinated lysine sites. ERAD components were found to be hyper-ubiquitinated after heat treatment, implying the feedback regulation of ERAD activity through protein degradation.

Keywords

endoplasmic reticulum; heat stress; maize; proteomics; ubiquitination.

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