A Clp/Hsp100 Chaperone Functions in Myxococcus xanthus Sporulation and Self-Organization

被引：5

作者：

Yan, Jinyuan ^{[1
]}

Garza, Anthony G. ^{[1
]}

Bradley, Michael D. ^{[1
]}

Welch, Roy D. ^{[1
]}

机构：

[1] Syracuse Univ, Dept Biol, Syracuse, NY 13244 USA

来源：

JOURNAL OF BACTERIOLOGY | 2012年 / 194卷 / 07期

基金：

美国国家科学基金会;

关键词：

SOCIAL GLIDING MOTILITY; FRUITING BODY FORMATION; LISTERIA-MONOCYTOGENES; EXTRACELLULAR FIBRILS; CLPC ATPASE; STAPHYLOCOCCUS-AUREUS; BACILLUS-SUBTILIS; CELL-INTERACTIONS; STRESS TOLERANCE; PROTEIN;

D O I：

10.1128/JB.06492-11

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The Clp/Hsp100 proteins are chaperones that play a role in protein degradation and reactivation. In bacteria, they exhibit a high degree of pleiotropy, affecting both individual and multicellular phenotypes. In this article, we present the first characterization of a Clp/Hsp100 homolog in Myxococcus xanthus (MXAN_4832 gene locus). Deletion of MXAN_4832 causes defects in both swarming and aggregation related to cell motility and the production of fibrils, which are an important component of the extracellular matrix of a swarm. The deletion also affects the formation of myxospores during development, causing them to become sensitive to heat. The protein product of MXAN_4832 can act as a chaperone in vitro, providing biochemical evidence in support of our hypothesis that MXAN_4832 is a functional Clp/Hsp100 homolog. There are a total of 12 Clp/Hsp100 homologs in M. xanthus, including MXAN_4832, and, based on its mutational and biochemical characterization, they may well represent an important group.

引用

页码：1689 / 1696

页数：8

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