一种耶尔森氏菌效应蛋白和一种绿脓杆菌无毒蛋白共同定义了一个在细菌致病过程中发挥作用的半胱氨酸蛋白酶家族。

A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis.

作者信息

Shao Feng, Merritt Peter M, Bao Zhaoqin, Innes Roger W, Dixon Jack E

机构信息

Department of Biological Chemistry, Medical School and Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.

出版信息

Cell. 2002 May 31;109(5):575-88. doi: 10.1016/s0092-8674(02)00766-3.

DOI:10.1016/s0092-8674(02)00766-3

PMID:12062101

Abstract

A Yersinia effector known as YopT and a Pseudomonas avirulence protein known as AvrPphB define a family of 19 proteins involved in bacterial pathogenesis. We show that both YopT and AvrPphB are cysteine proteases, and their proteolytic activities are dependent upon the invariant C/H/D residues conserved in the entire YopT family. YopT cleaves the posttranslationally modified Rho GTPases near their carboxyl termini, releasing them from the membrane. This leads to the disruption of actin cytoskeleton in host cells. The proteolytic activity of AvrPphB is essential for autoproteolytic cleavage of an AvrPphB precursor as well as for eliciting the hypersensitive response in plants. These findings provide new insights into mechanisms of animal and plant pathogenesis.

摘要

一种名为YopT的耶尔森氏菌效应蛋白和一种名为AvrPphB的假单胞菌无毒蛋白定义了一个由19种参与细菌致病过程的蛋白质组成的家族。我们发现YopT和AvrPphB都是半胱氨酸蛋白酶，它们的蛋白水解活性依赖于整个YopT家族中保守的不变C/H/D残基。YopT在翻译后修饰的Rho GTP酶的羧基末端附近进行切割，使其从膜上释放出来。这导致宿主细胞中肌动蛋白细胞骨架的破坏。AvrPphB的蛋白水解活性对于AvrPphB前体的自蛋白水解切割以及引发植物中的过敏反应至关重要。这些发现为动物和植物致病机制提供了新的见解。