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

• DOI: 10.1186/s12870-022-03964-4
• Publication Date: 2022-12-24T02:02:33Z
• Authors: Jianfei Guo; Zhigang Ma; Ce Deng; Junqiang Ding; Yuxiao Chang
• Keywords: Proteostasis; Proteome

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