Identification and characterization of an endolysin encoded by the Streptomyces aureofaciens phage mu 1/6
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15058185
DOI
10.1007/bf02931507
Knihovny.cz E-resources
- MeSH
- Bacteriophage mu enzymology genetics MeSH
- Cell Wall metabolism MeSH
- Endopeptidases genetics isolation & purification metabolism MeSH
- Hydrolysis MeSH
- Cloning, Molecular MeSH
- Hydrogen-Ion Concentration MeSH
- Molecular Sequence Data MeSH
- Gene Expression Regulation, Viral MeSH
- Gene Expression Regulation, Enzymologic MeSH
- Amino Acid Sequence MeSH
- Streptomyces aureofaciens virology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- endolysin MeSH Browser
- Endopeptidases MeSH
An open reading frame homologous to the genes encoding several cell-wall hydrolyzing enzymes was identified on the genome of actinophage mu 1/6. This open reading frame encoding the putative endolysin was amplified by polymerase chain reaction and cloned into the expression vector pET-21a. This gene consisted of 1182 bp encoding a 393 amino acid polypeptide with a molar mass of 42.1 kDa. The gene product was overexpressed in Escherichia coli, and then the lytic enzyme was purified by a two-step chromatographic procedure. When applied exogenously, the endolysin of phage mu 1/6 was active against all tested Streptomyces strains but did not affect other bacteria. The amino acid sequence showed a high homology with a putative amidase of the Streptomyces phase phi C31. Downstream of the endolysin gene, an open reading frame encoding an 88 amino acid protein was identified. Structural analysis of its sequence revealed features characteristics for holin.
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Complete genome sequence and analysis of the Streptomyces aureofaciens phage mu1/6
