A comprehensive dynamic immune acetylproteomics profiling induced by Puccinia polysora in maize

BMC Plant Biology

Research

Ce Deng¹  Junqiang Ding¹  Jianfei Guo²  Yuxiao Chang²  Zhigang Ma³ 

[1] College of Agronomy, Henan Agricultural University, 450046, Zhengzhou, China;The State Key Laboratory of Wheat and Maize Crop Science and Center for Crop Genome Engineering, Henan Agricultural University, 450046, Zhengzhou, China;Shenzhen Branch, Guangdong Laboratory of Lingnan Modern Agriculture, Genome Analysis Laboratory of the Ministry of Agriculture and Rural Affairs, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, 518120, Shenzhen, China;Shenzhen Branch, Guangdong Laboratory of Lingnan Modern Agriculture, Genome Analysis Laboratory of the Ministry of Agriculture and Rural Affairs, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, 518120, Shenzhen, China;State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, 475004, Kaifeng, China;Shenzhen Research Institute of Henan university, 518000, Shenzhen, China;

关键词: Southern corn rust (SCR);    Mass spectrometry;    Quantitative proteomics;    Lysine acetylation;    Plant-pathogen interaction;    Immune response;    Puccinia polysora;   

DOI  :  10.1186/s12870-022-03964-4

 received in 2022-08-29, accepted in 2022-11-25,  发布年份 2022

来源: Springer

【 摘 要 】

Lysine-ε-acetylation (Kac) is a reversible post-translational modification that plays important roles during plant-pathogen interactions. Some pathogens can deliver secreted effectors encoding acetyltransferases or deacetylases into host cell to directly modify acetylation of host proteins. However, the function of these acetylated host proteins in plant-pathogen defense remains to be determined. Employing high-resolution tandem mass spectrometry, we analyzed protein abundance and lysine acetylation changes in maize infected with Puccinia polysora (P. polysora) at 0 h, 12 h, 24 h, 48 h and 72 h. A total of 7412 Kac sites from 4697 proteins were identified, and 1732 Kac sites from 1006 proteins were quantified. Analyzed the features of lysine acetylation, we found that Kac is ubiquitous in cellular compartments and preferentially targets lysine residues in the -F/W/Y-X-X-K (ac)-N/S/T/P/Y/G- motif of the protein, this Kac motif contained proteins enriched in basic metabolism and defense-associated pathways during fungal infection. Further analysis of acetylproteomics data indicated that maize regulates cellular processes in response to P. polysora infection by altering Kac levels of histones and non-histones. In addition, acetylation of pathogen defense-related proteins presented converse patterns in signaling transduction, defense response, cell wall fortification, ROS scavenging, redox reaction and proteostasis. Our results provide informative resources for studying protein acetylation in plant-pathogen interactions, not only greatly extending the understanding on the roles of acetylation in vivo, but also providing a comprehensive dynamic pattern of Kac modifications in the process of plant immune response.

【 授权许可】

CC BY   
© The Author(s) 2022

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