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PMID: 7559367 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Molecular characterization and functional analysis of the major autolysin of Staphylococcus aureus 8325/4.

Journal of bacteriology ·Vol. 177 ·No. 19 ·1995-10-00 ·Pages 5723-5

Foster SJ

Abstract

The gene encoding the major autolysin of Staphylococcus aureus 8325/4 has been cloned, sequenced, and insertionally inactivated. The three-domain, 137,384-Da protein has a C-terminal glucosaminidase active site and is involved in cell separation, generalized cell lysis, and release of wall material at the cell surface. Expression occurs throughout growth and is stimulated by low temperatures and in the presence of 1 M NaCl.

MeSH Terms
Binding Sites Cell Wall/enzymology Cloning, Molecular Gene Expression Regulation, Bacterial/drug effects Genes, Bacterial/genetics Hexosaminidases/metabolism Molecular Sequence Data Mutation N-Acetylmuramoyl-L-alanine Amidase/genetics,metabolism Recombinant Fusion Proteins/biosynthesis Restriction Mapping Sequence Analysis, DNA Sodium Chloride/pharmacology Staphylococcus aureus/enzymology,genetics Temperature
Chemicals
Recombinant Fusion Proteins Sodium Chloride Hexosaminidases N-Acetylmuramoyl-L-alanine Amidase
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Foster S J
Department of Molecular Biology and Biotechnology, University of Sheffield, United Kingdom.
References (18)
18 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.177.19.5723-5725.1995
Published
1995-10-00
Pages
5723-5
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC177389
Subset
IM
Databases
GENBANK
L41499
External Links
PubMed source DOI: 10.1128/jb.177.19.5723-5725.1995 PMC Full Text View journal details
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