A mutation of Escherichia coli SecA protein that partially compensates for the absence of SecB. release_z6eca72hovae3bu4qncmi7soyq

by L McFarland, O Francetić, C A Kumamoto

Published in Journal of Bacteriology by American Society for Microbiology.

1993   Volume 175, p2255-2262


The Escherichia coli SecB protein is a cytosolic chaperone protein that is required for rapid export of a subset of exported proteins. To aid in elucidation of the activities of SecB that contribute to rapid export kinetics, mutations that partially suppressed the export defect caused by the absence of SecB were selected. One of these mutations improves protein export in the absence of SecB and is the result of a duplication of SecA coding sequences, leading to the synthesis of a large, in-frame fusion protein. Unexpectedly, this mutation conferred a second phenotype. The secA mutation exacerbated the defective protein export caused by point mutations in the signal sequence of pre-maltose-binding protein. One explanation for these results is that the mutant SecA protein has sustained a duplication of its binding site(s) for exported protein precursors so that the mutant SecA is altered in its interaction with precursor molecules.
In application/xml+jats format

Archived Files and Locations

application/pdf  2.1 MB
web.archive.org (webarchive)
jb.asm.org (web)
application/pdf  2.1 MB
jb.asm.org (web)
web.archive.org (webarchive)
Read Archived PDF
Type  article-journal
Stage   published
Year   1993
Language   en ?
Journal Metadata
Not in DOAJ
In Keepers Registery
ISSN-L:  0021-9193
Work Entity
access all versions, variants, and formats of this works (eg, pre-prints)
Catalog Record
Revision: d17c895a-05fe-463d-893c-befedb0b4252