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Cited by 217

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli.

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Wolfe, P B, Rice, M, Wickner, W·1985·Journal of Biological Chemistry

Abstract

We have examined the effects of thermosensitive mutations in secA and secY (prlA) genes on the export of proteins to the three layers of the Escherichia coli cell surface. After several hours at the nonpermissive temperature, the export of two major outer membrane proteins, lipoprotein and OmpA, is delayed, then essentially blocked, in either a secA or secY strain. These mutations also have a strong effect on the export of several proteins, such as maltose binding protein, to the periplasm, though the export of many periplasmic proteins is not affected. secA and secY block the assembly of leader peptidase, which is made without a leader sequence, into the inner membrane. However, the membrane assembly of M13 coat protein (an inner membrane protein made with an amino-terminal leader sequence) is not affected. Thus, the requirement for sec function for export does not correlate with the presence or absence of leader peptide or with a particular subcellular compartment, but rather is specific to each particular protein.

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Metadata

Authors
Wolfe, P. B., Rice, M., & Wickner, W.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1985-02
Volume
260
Issue
3
Pages
1836-1841
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1550654653
Cited by
217
References
1
FWCI
10.68
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli. https://app.cochat.ai/papers/10.1016/s0021-9258(18)89669-7
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Wolfe, P. B., Rice, M., & Wickner, W. (1985). Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)89669-7

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