Distinct mutation sites in prlA suppressor mutant strains of Escherichia coli respond either to suppression of signal peptide mutations or to blockage of staphylokinase processing.

Journal of bacteriology ·Vol. 170 ·No. 11 ·1988-11-00 ·Pages 5389-91

Sako T, Iino T

Abstract

We have cloned and sequenced some prlA mutant alleles of the Escherichia coli secY gene. From the mutation sites determined, it is strongly suggested that distinct regions in the SecY (PrlA) protein are involved in the recognition of different structural features of a signal peptide as it functions.

MeSH Terms

Alleles Bacterial Proteins/genetics Cloning, Molecular Escherichia coli/genetics Genes Genes, Bacterial Metalloendopeptidases/genetics Mutation Protein Conformation Suppression, Genetic

Chemicals

Bacterial Proteins Metalloendopeptidases auR protein, Staphylococcus aureus

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Sako T

Yakult Central Institute for Microbiological Research, Tokyo, Japan.

Iino T

References (25)

25 references, click to expand

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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

0021-9193

DOI

10.1128/jb.170.11.5389-5391.1988

Published

1988-11-00

Pages

5389-91

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC211621

Subset

External Links

PubMed source DOI: 10.1128/jb.170.11.5389-5391.1988 PMC Full Text View journal details

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Distinct mutation sites in prlA suppressor mutant strains of Escherichia coli respond either to suppression of signal peptide mutations or to blockage of staphylokinase processing.

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