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Nucleic Acids Res. 2001 Feb 15;29(4):914-20.

Identification and properties of the crenarchaeal single-stranded DNA binding protein from Sulfolobus solfataricus.

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  • 1Centre for Biomolecular Science, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK.

Abstract

Single-stranded DNA binding proteins (SSBs) play central roles in cellular and viral processes involving the generation of single-stranded DNA. These include DNA replication, homologous recombination and DNA repair pathways. SSBs bind DNA using four 'OB-fold' (oligonucleotide/oligosaccharide binding fold) domains that can be organised in a variety of overall quaternary structures. Thus eubacterial SSBs are homotetrameric whilst the eucaryal RPA protein is a heterotrimer and euryarchaeal proteins vary significantly in their subunit compositions. We demonstrate that the crenarchaeal SSB protein is an abundant protein with a unique structural organisation, existing as a monomer in solution and multimerising on DNA binding. The protein binds single-stranded DNA distributively with a binding site size of approximately 5 nt per monomer. Sulfolobus SSB lacks the zinc finger motif found in the eucaryal and euryarchaeal proteins, possessing instead a flexible C-terminal tail, sensitive to trypsin digestion, that is not required for DNA binding. In comparison with Escherichia coli SSB, the tail may play a role in protein-protein interactions during DNA replication and repair.

PMID:
11160923
[PubMed - indexed for MEDLINE]
PMCID:
PMC29618
Free PMC Article
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