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PMID: 2202591 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Mapping of catalytically important domains in Escherichia coli leader peptidase.

The EMBO journal ·Vol. 9 ·No. 9 ·1990-09-00 ·Pages 2717-22

Bilgin N, Lee JI, Zhu HY, Dalbey R, von Heijne G

Abstract

Leader peptidase (Lep) is a central component of the secretory machinery of Escherichia coli, where it serves to remove signal peptides from secretory proteins. It spans the inner membrane twice with a large C-terminal domain protruding into the periplasmic space. To investigate the importance of the different structural domains for the catalytic activity, we have studied the effects of a large panel of Lep mutants on the processing of signal peptides, both in vivo and in vitro. Our data suggest that the first transmembrane and cytoplasmic regions are not directly involved in catalysis, but that the second transmembrane region and the region immediately following it may be in contact with the signal peptide and/or located spatially close to the active site of Lep.

MeSH Terms
Amino Acid Sequence Bacterial Outer Membrane Proteins/genetics Capsid/genetics Cell Membrane/enzymology Coliphages/genetics,metabolism Cytoplasm/enzymology Endopeptidases/genetics,metabolism Escherichia coli/enzymology,genetics Kinetics Membrane Proteins Molecular Sequence Data Mutation Protein Conformation Protein Processing, Post-Translational Serine Endopeptidases
Chemicals
Bacterial Outer Membrane Proteins Membrane Proteins Endopeptidases Serine Endopeptidases type I signal peptidase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Bilgin N
Department of Molecular Biology, Karolinska Institute Center for Biotechnology, NOVUM, Huddinge, Sweden.
Lee J I
Zhu H Y
Dalbey R
von Heijne G
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1990-09-00
Pages
2717-22
Language
English
Region
England
NLM ID
8208664
PMCID
PMC551978
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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