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

R. I M Wadsworth, M. F. White*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

115 Citations (Scopus)

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 ∼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.

Original languageEnglish
Pages (from-to)914-920
Number of pages7
JournalNucleic Acids Research
Volume29
Issue number4
Publication statusPublished - 15 Feb 2001

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