A distinct single-stranded DNA-binding protein encoded by the Lactococcus lactis bacteriophage bIL67.
Virology
; 363(1): 104-12, 2007 Jun 20.
Article
en En
| MEDLINE
| ID: mdl-17316735
ABSTRACT
Single-stranded binding proteins (SSBs) are found to participate in various processes of DNA metabolism in all known organisms. We describe here a SSB protein encoded by the Lactococcus lactis phage bIL67 orf14 gene. It is the first noted attempt at characterizing a SSB protein from a lactococcal phage. The purified Orf14(bIL67) binds unspecifically to ssDNA with the same high affinity as the canonical Bacillus subtilis SSB. Electrophoretic mobility-shift assays performed with mutagenized Orf14(bIL67) protein derivatives suggest that ssDNA-binding occurs via a putative OB-fold structure predicted by three-dimensional modeling. The native Orf14(bIL67) forms homotetramers as determined by gel filtration studies. These results allow distinguishing the first lactococcal phage protein with single-strand binding affinity, which defines a novel cluster of phage SSBs proteins. The possible role of Orf14(bIL67) in phage multiplication cycle is also discussed.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Bacteriófagos
/
Proteínas Virales
/
ADN de Cadena Simple
/
Lactococcus lactis
/
Proteínas de Unión al ADN
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Virology
Año:
2007
Tipo del documento:
Article
País de afiliación:
Francia