Protein acetylation and deacetylation in plant-pathogen interactions

被引:11
作者
Wang, Jing [1 ,2 ]
Liu, Chao [1 ,2 ]
Chen, Yun [1 ,2 ]
Zhao, Youfu [3 ]
Ma, Zhonghua [1 ,2 ]
机构
[1] Zhejiang Univ, State Key Lab Rice Biol, Inst Biotechnol, Hangzhou, Peoples R China
[2] Zhejiang Univ, Inst Biotechnol, Key Lab Mol Biol Crop Pathogens & Insects, Hangzhou, Peoples R China
[3] Univ Illinois, Dept Crop Sci, Urbana, IL USA
基金
中国国家自然科学基金;
关键词
GCN5-RELATED N-ACETYLTRANSFERASES; DEFENSE-RELATED GENES; HISTONE ACETYLTRANSFERASE; LYSINE ACETYLATION; CATALYTIC MECHANISM; ASEXUAL DEVELOPMENT; MOLECULAR-BASIS; CELL-DEATH; RESPONSES; VIRULENCE;
D O I
10.1111/1462-2920.15725
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:4841 / 4855
页数:15
相关论文
共 111 条
  • [1] A rapid and sensitive assay for histone acetyl-transferase activity
    Ait-Si-Ali, S
    Ramirez, S
    Robin, P
    Trouche, D
    Harel-Bellan, A
    [J]. NUCLEIC ACIDS RESEARCH, 1998, 26 (16) : 3869 - 3870
  • [2] ACETYLATION + METHYLATION OF HISTONES + THEIR POSSIBLE ROLE IN REGULATION OF RNA SYNTHESIS
    ALLFREY, VG
    FAULKNER, R
    MIRSKY, AE
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1964, 51 (05) : 786 - +
  • [3] Mechanism of sirtuin inhibition by nicotinamide:: Altering the NAD+ cosubstrate specificity of a Sir2 enzyme
    Avalos, JL
    Bever, KM
    Wolberger, C
    [J]. MOLECULAR CELL, 2005, 17 (06) : 855 - 868
  • [4] Plant β-1,3-glucanases: their biological functions and transgenic expression against phytopathogenic fungi
    Balasubramanian, Vaiyapuri
    Vashisht, Divya
    Cletus, Jean
    Sakthivel, Natarajan
    [J]. BIOTECHNOLOGY LETTERS, 2012, 34 (11) : 1983 - 1990
  • [5] Regulation of chromatin by histone modifications
    Bannister, Andrew J.
    Kouzarides, Tony
    [J]. CELL RESEARCH, 2011, 21 (03) : 381 - 395
  • [6] Cooperation between SAGA and SWI/SNF complexes is required for efficient transcriptional responses regulated by the yeast MAPK Slt2
    Belen Sanz, Ana
    Garcia, Raul
    Manuel Rodriguez-Pena, Jose
    Nombela, Cesar
    Arroyo, Javier
    [J]. NUCLEIC ACIDS RESEARCH, 2016, 44 (15) : 7159 - 7172
  • [7] Catalytic mechanism of a MYST family histone acetyltransferase
    Berndsen, Christopher E.
    Albaugh, Brittany N.
    Tan, Song
    Denu, John M.
    [J]. BIOCHEMISTRY, 2007, 46 (03) : 623 - 629
  • [8] Histone Acetyltransferases in Plant Development and Plasticity
    Boycheva, Irina
    Vassileva, Valya
    Iantcheva, Anelia
    [J]. CURRENT GENOMICS, 2014, 15 (01) : 28 - 37
  • [9] A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors
    Burger, Marco
    Willige, Bjorn C.
    Chory, Joanne
    [J]. NATURE COMMUNICATIONS, 2017, 8
  • [10] Regulation, Function, and Detection of Protein Acetylation in Bacteria
    Carabetta, Valerie J.
    Cristea, Ileana M.
    [J]. JOURNAL OF BACTERIOLOGY, 2017, 199 (16)