Nucleic Acids Research, 2001, Vol. 29, No. 4 914-920
© 2001 Oxford University Press
Identification and properties of the crenarchaeal single-stranded DNA binding protein from Sulfolobus solfataricus
Centre for Biomolecular Science, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK
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 ~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.
* To whom correspondence should be addressed. Tel: +44 1334 463432; Fax: +44 1334 462595; Email: mfw2{at}st-andrews.ac.uk
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