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PMID: 8550430 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Serine protease EpiP from Staphylococcus epidermidis catalyzes the processing of the epidermin precursor peptide.

Journal of bacteriology ·Vol. 178 ·No. 1 ·1996-01-00 ·Pages 284-8

Geissler S, Götz F, Kupke T

Abstract

The function of serine protease EpiP in epidermin biosynthesis was investigated. Epidermin is synthesized as a 52-amino-acid precursor peptide, EpiA, which is posttranslationally modified and processed to the mature 22-amino-acid peptide antibiotic. epiP was expressed in Staphylococcus carnosus with xylose-regulated expression vector pCX15. The cleavage of the unmodified EpiA precursor peptide to leader peptide and proepidermin by EpiP-containing culture filtrates of S. carnosus (pCX15epiP) was followed by reversed-phase chromatography and subsequent electrospray mass spectrometry.

MeSH Terms
Amino Acid Sequence Anti-Bacterial Agents/biosynthesis Bacteriocins Base Sequence Enzyme Induction/drug effects Molecular Sequence Data Peptides Protein Precursors/metabolism Protein Processing, Post-Translational/physiology Protein Sorting Signals Recombinant Fusion Proteins/biosynthesis Sequence Analysis Serine Endopeptidases/biosynthesis,genetics,isolation & purification,metabolism Staphylococcus/genetics Staphylococcus epidermidis/enzymology Xylose/pharmacology
Chemicals
Anti-Bacterial Agents Bacteriocins Peptides Protein Precursors Protein Sorting Signals Recombinant Fusion Proteins epidermin Xylose EpiP serine protease Serine Endopeptidases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Geissler S
Universität Tübingen, Federal Republic of Germany.
Götz F
Kupke T
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.178.1.284-288.1996
Published
1996-01-00
Pages
284-8
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC177651
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.178.1.284-288.1996 PMC Full Text View journal details
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