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Signal peptide protection by specific chaperone.

Abstract：

:TorD is the private chaperone of TorA, a periplasmic respiratory molybdoenzyme of Escherichia coli. In this study, it is demonstrated that TorD is required to maintain the integrity of the twin-arginine signal sequence of the cytoplasmic TorA precursors. In the absence of TorD, 35 out of the 39 amino acid residues of the signal peptide were lost and the proteolysis of the N-terminal extremity of TorA precursors was not prevented by the molybdenum cofactor insertion. We thus propose that one of the main roles of TorD is to protect the TorA signal peptide to allow translocation of the enzyme by the TAT system.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Genest O,Seduk F,Ilbert M,Méjean V,Iobbi-Nivol C

doi

10.1016/j.bbrc.2005.11.107

subject

Has Abstract

pub_date

2006-01-20 00:00:00

pages

991-5

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02646-X

journal_volume

339

pub_type

杂志文章

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