ArticleFolia microbiologica2003
Identification and characterization of an endolysin encoded by the Streptomyces aureofaciens phage mu 1/6.
Article in Folia microbiologica, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Characterization of the N-Terminal Catalytic Domain of Lytµ1/6, an Endolysin from Streptomyces aureofaciens Phage µ1/6.Current microbiology · 2016Article
- Learning from bacteriophages - advantages and limitations of phage and phage-encoded protein applications.Current protein & peptide science · 2012Review
- Analysis of the site-specific integration system of the Streptomyces aureofaciens phage μ1/6.Current microbiology · 2012Article
- Thermal stability of Cpl-7 endolysin from the streptococcus pneumoniae bacteriophage Cp-7; cell wall-targeting of its CW_7 motifs.PloS one · 2012Article
- The lysis system of the Streptomyces aureofaciens phage mu1/6.Current microbiology · 2008Article
- Complete genome sequence and analysis of the Streptomyces aureofaciens phage mu1/6.Folia microbiologica · 2007Article
- Identification of a holin encoded by the Streptomyces aureofaciens phage micro1/6; functional analysis in Escherichia coli system.Folia microbiologica · 2004Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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