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PMID: 3285342 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 85 ·No. 10 ·1988-05-00 ·Pages 3363-6

von Heijne G, Wickner W, Dalbey RE

Abstract

Leader peptidase is an integral, transmembrane protein of the plasma membrane of Escherichia coli. Its membrane assembly requires its internal, uncleaved signal sequence, its large periplasmic carboxyl-terminal region, and an apolar domain that is known as a "hydrophobic helper." We now show that the polar cytoplasmic domain of leader peptidase is a unique membrane assembly element, which we term a "translocation poison" sequence. This sequence is defined by its ability to block the action of a signal sequence that either precedes or follows it. To our knowledge, this is the first entirely polar topogenic element. Deletion analysis shows that the role of the leader peptidase hydrophobic helper sequence in its membrane assembly is to overcome the block to assembly caused by the poison sequence.

MeSH Terms
Cell Membrane/enzymology Endopeptidases/genetics Escherichia coli/enzymology,genetics Membrane Proteins Mutation Plasmids Protein Processing, Post-Translational Serine Endopeptidases
Chemicals
Membrane Proteins Endopeptidases Serine Endopeptidases type I signal peptidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
von Heijne G
Molecular Biology Institute, University of California, Los Angeles 90024.
Wickner W
Dalbey R E
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27 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.85.10.3363
Published
1988-05-00
Pages
3363-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC280209
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.85.10.3363 PMC Full Text View journal details
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