A distinct single-stranded DNA-binding protein encoded by the Lactococcus lactis bacteriophage bIL67

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 lacto...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2007-06, Vol.363 (1), p.104-112
Main Authors: Szczepaǹska, Agnieszka K, Bidnenko, Elena, Płochocka, Danuta, McGovern, Stephen, Ehrlich, S. Dusko, Bardowski, Jacek, Polard, Patrice, Chopin, Marie-Christine
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacillus subtilis
Bacteriophage
Bacteriophages - genetics
Bacteriophages - metabolism
DNA recombination
DNA, Single-Stranded - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - isolation & purification
DNA-Binding Proteins - metabolism
Infectious Disease
Lactococcus lactis
Lactococcus lactis - virology
Models, Molecular
Molecular Sequence Data
OB-fold
Protein Structure, Quaternary
Single-strand binding protein
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - isolation & purification
Viral Proteins - metabolism
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Summary: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 Orf14bIL67 binds unspecifically to ssDNA with the same high affinity as the canonical Bacillus subtilis SSB. Electrophoretic mobility-shift assays performed with mutagenized Orf14bIL67 protein derivatives suggest that ssDNA-binding occurs via a putative OB-fold structure predicted by three-dimensional modeling. The native Orf14bIL67 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 Orf14bIL67 in phage multiplication cycle is also discussed.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2007.01.023