TY - JOUR
T1 - Protein Acetylation and Deacetylation in Plant-pathogen Interactions
AU - Wang, Jing
AU - Liu, Chao
AU - Chen, Yun
AU - Zhao, Youfu
AU - Ma, Zhonghua
N1 - Funding Information:
This research was supported by Science and Technology Project of Zhejiang Province (2018C02G2011110), National Natural Science Foundation of China (31930088), and China Agriculture Research System of MOF and MARAC (CARS‐3‐1‐29).
Publisher Copyright:
© 2021 Society for Applied Microbiology and John Wiley & Sons Ltd.
PY - 2021/9
Y1 - 2021/9
N2 - Protein acetylation and deacetylation catalysed by lysine acetyltransferases (KATs) and deacetylases (KDACs), respectively, are major mechanisms regulating various cellular processes. During the fight between microbial pathogens and host plants, both apply a set of measures, including acetylation interference, to strengthen themselves while suppressing the other. In this review, we first summarize KATs and KDACs in plants and their pathogens. Next, we introduce diverse acetylation and deacetylation mechanisms affecting protein functions, including the regulation of enzyme activity and specificity, protein–protein or protein-DNA interactions, subcellular localization and protein stability. We then focus on the current understanding of acetylation and deacetylation in plant–pathogen interactions. Additionally, we also discuss potential acetylation-related approaches for controlling plant diseases.
AB - Protein acetylation and deacetylation catalysed by lysine acetyltransferases (KATs) and deacetylases (KDACs), respectively, are major mechanisms regulating various cellular processes. During the fight between microbial pathogens and host plants, both apply a set of measures, including acetylation interference, to strengthen themselves while suppressing the other. In this review, we first summarize KATs and KDACs in plants and their pathogens. Next, we introduce diverse acetylation and deacetylation mechanisms affecting protein functions, including the regulation of enzyme activity and specificity, protein–protein or protein-DNA interactions, subcellular localization and protein stability. We then focus on the current understanding of acetylation and deacetylation in plant–pathogen interactions. Additionally, we also discuss potential acetylation-related approaches for controlling plant diseases.
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U2 - 10.1111/1462-2920.15725
DO - 10.1111/1462-2920.15725
M3 - Review article
C2 - 34398483
AN - SCOPUS:85113788530
SN - 1462-2912
VL - 23
SP - 4841
EP - 4855
JO - Environmental Microbiology
JF - Environmental Microbiology
IS - 9
ER -