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细菌对 OTU 去泛素化酶结构域的篡夺。

Bacterial usurpation of the OTU deubiquitinase fold.

机构信息

Department of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, USA.

Department of Microbiology, Graduate School of Medicine, Gifu University, Japan.

出版信息

FEBS J. 2024 Aug;291(15):3303-3316. doi: 10.1111/febs.16725. Epub 2023 Jan 24.

Abstract

The extensive cellular signalling events controlled by posttranslational ubiquitination are tightly regulated through the action of specialized proteases termed deubiquitinases. Among them, the OTU family of deubiquitinases can play very specialized roles in the regulation of discrete subtypes of ubiquitin signals that control specific cellular functions. To exert control over host cellular functions, some pathogenic bacteria have usurped the OTU deubiquitinase fold as a secreted virulence factor that interferes with ubiquitination inside infected cells. Herein, we provide a review of the function of bacterial OTU deubiquitinases during infection, the structural basis for their deubiquitinase activities and the bioinformatic approaches leading to their identification. Understanding bacterial OTU deubiquitinases holds the potential for discoveries not only in bacterial pathogenesis but in eukaryotic biology as well.

摘要

泛素化的翻译后细胞信号事件受到高度调控,这种调控是通过专门的蛋白酶(称为去泛素化酶)来实现的。其中,OTU 家族的去泛素化酶可以在调节控制特定细胞功能的离散泛素信号亚型方面发挥非常特殊的作用。为了对宿主细胞功能进行控制,一些致病菌盗用了 OTU 去泛素化酶折叠作为一种分泌的毒力因子,该因子会干扰感染细胞内的泛素化。本文综述了细菌 OTU 去泛素化酶在感染过程中的功能、其去泛素化酶活性的结构基础以及导致其鉴定的生物信息学方法。了解细菌 OTU 去泛素化酶不仅有可能揭示细菌发病机制,还有可能揭示真核生物学的奥秘。

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