Affiliation:
1. Department of Microbiology & Immunology, University of California-Los Angeles School of Medicine, Los Angeles, California 90095
Abstract
ABSTRACT
Pathogenic yersiniae secrete 14 Yop proteins via the type III pathway. Synthesis of YopQ occurs when the type III machinery is activated by a low-calcium signal, but not when the calcium concentration is above 100 μM. To characterize the mechanism that regulates the expression of
yopQ
, mutants that permit synthesis of YopQ in the presence of calcium were isolated. Yersiniae bearing deletion mutations in
yopN
,
tyeA
,
sycN
, or
yscB
synthesized and secreted YopQ in both the presence and the absence of calcium. In contrast, yersiniae with a deletion in
yopD
or
lcrH
synthesized YopQ in the presence of calcium but did not secrete the polypeptide. These variants displayed no defect in YopQ secretion under low-calcium conditions, revealing that
yopD
and
lcrH
are required for the regulation of
yopQ
expression. Experiments with transcriptional and translational fusions to the
npt
reporter gene suggest that
yopD
and
lcrH
regulate
yopQ
expression at a posttranscriptional step. YopD and LcrH form a complex in the bacterial cytosol and bind
yopQ
mRNA. Models that can account for posttranscriptional regulatory mechanisms of
yop
expression are discussed.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
88 articles.
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