细菌ADP-核糖基水解酶的结构基础与催化机理
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国家自然科学基金(82225028,82172287,31900879,32171265);国家重点研发计划(2021YFC2301403)


Structural basis and catalytic mechanism of bacterial ADP-ribosyl hydrolases
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    摘要:

    ADP-核糖基化(adenosine diphosphate-ribosylation,ADPr)修饰是由ADP-核糖基转移酶(adenosine diphosphate-ribosyltransferases,ARTs)和ADP-核糖基水解酶(adenosine diphosphate-ribosylhydrolases,ARHs)共同催化的可逆化翻译后修饰,广泛地分布于真核生物和原核生物中。ARHs是一类能够逆转特定氨基酸残基或DNA、RNA特定位点/序列ADPr修饰的关键酶,通过调控细菌或宿主的生理代谢、信号传导和基因表达调控等关键生命过程,在细菌物种间/种内的竞争、应激反应和致病性中发挥重要作用。鉴于细菌ARHs相关研究领域近期取得了一定的进展,本综述从其分类、结构特点以及催化机制角度对其进行系统总结,以期为深入理解细菌ARHs的作用机理及其在细菌生命过程的重要生物学功能提供帮助。

    Abstract:

    Adenosine diphosphate-ribosylation (ADPr) is a reversible post-translational modification that is catalyzed by adenosine diphosphate-ribosyltransferases (ARTs) and adenosine diphosphate- ribosylhydrolases (ARHs), and it widely occurs in eukaryotes and prokaryotes. ARHs are a class of key enzymes that can reverse ADPr modification of specific amino acid residues or specific sites/sequences of DNA and RNA. They can regulate the physiological metabolism, signal transduction, gene expression, and other key life processes in bacteria or hosts, playing an important role in the inter/intraspecific competition, stress responses, and pathogenicity of bacteria. This article reviews the classification, structural characteristics, and catalytic mechanisms of bacterial ARHs, aiming to enrich our understanding about the catalytic mechanisms and biological functions of ARHs in bacterial life.

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焦引弟,张路豪,欧阳松应,关洪鑫. 细菌ADP-核糖基水解酶的结构基础与催化机理. 微生物学报, 2025, 65(1): 38-51

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  • 收稿日期:2024-08-19
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  • 在线发布日期: 2025-01-04
  • 出版日期: 2025-01-04
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