Affiliation:
1. Department of Microbiology and Immunology
2. Department of Biochemistry and Molecular Biology, University of Miami, Miller School of Medicine, Miami, Florida
Abstract
ABSTRACT
Yersinia
spp. use a type 3 secretion system (T3SS) to directly inject six proteins into macrophages, and any impairment of this process results in a profound reduction in virulence. We previously showed that the exoribonuclease polynucleotide phosphorylase (PNPase) was required for optimal T3SS functioning in
Yersinia pseudotuberculosis
and
Yersinia pestis
. Here we report that
Y. pseudotuberculosis
cells with reduced RNase E activity are likewise impaired in T3SS functioning and that phenotypically they resemble Δ
pnp
cells. RNase E does not affect expression levels of the T3SS substrates but instead, like PNPase, regulates a terminal event in the secretion pathway. This similarity, together with the fact that RNase E and PNPase can be readily copurified from
Y. pseudotuberculosis
cell extracts, suggests that these two RNases regulate T3SS activity through a common mechanism. This is the first report that RNase E activity impacts the T3SS as well as playing a more general role in infectivity.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
44 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献