Functions and mechanisms of non‐histone protein acetylation in plants

Author:

Jin Xia1ORCID,Li Xiaoshuang2ORCID,Teixeira da Silva Jaime A.3ORCID,Liu Xuncheng1ORCID

Affiliation:

1. Guangdong Provincial Key Laboratory of Applied Botany, Key Laboratory of South China Agricultural Plant Molecular Analysis and Genetic Improvement South China Botanical Garden, Chinese Academy of Sciences Guangzhou 510650 China

2. State Key Laboratory of Desert and Oasis Ecology, Key Laboratory of Ecological Safety and Sustainable Development in Arid Lands Xinjiang Institute of Ecology and Geography, Chinese Academy of Sciences Urumqi 830000 China

3. Independent Researcher Miki‐cho 761‐0799 Kagawa‐ken Japan

Abstract

ABSTRACTLysine acetylation, an evolutionarily conserved post‐translational protein modification, is reversibly catalyzed by lysine acetyltransferases and lysine deacetylases. Lysine acetylation, which was first discovered on histones, mainly functions to configure the structure of chromatin and regulate gene transcriptional activity. Over the past decade, with advances in high‐resolution mass spectrometry, a vast and growing number of non‐histone proteins modified by acetylation in various plant species have been identified. Lysine acetylation of non‐histone proteins is widely involved in regulating biological processes in plants such as photosynthesis, energy metabolism, hormone signal transduction and stress responses. Moreover, in plants, lysine acetylation plays crucial roles in regulating enzyme activity, protein stability, protein interaction and subcellular localization. This review summarizes recent progress in our understanding of the biological functions and mechanisms of non‐histone protein acetylation in plants. Research prospects in this field are also noted.

Funder

National Natural Science Foundation of China

Publisher

Wiley

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