Affiliation:
1. Department of Molecular Biology and Biochemistry, Wesleyan University, Middletown, Connecticut 06459
Abstract
ABSTRACT
SecA is an ATPase and motor protein that drives protein translocation across the bacterial plasma membrane. In
Escherichia coli
SecA levels are regulated by the secretion needs of the cell utilizing
secM
, which encodes a secreted protein. Previous studies demonstrated that this regulation requires a translational pause within
secM
, whose duration regulates the accessibility of the
secA
Shine-Dalgarno sequence on
secM secA
mRNA. Here we provide evidence that translocon “pulling” of nascent SecM is what regulates the duration of the
secM
translational pause, and thus
secA
expression levels, thereby providing direct support for this model.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
92 articles.
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