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A distinctive single-stranded DNA-binding protein from the Archaeon Sulfolobus solfataricus by Cynthia A. Haseltine; Stephen C. Kowalczykowski is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Summary Single‐stranded DNA binding proteins (SSBs) have been identified in all three domains of life. Here, we report the identification of a novel crenarchaeal SSB protein that is distinctly different from its euryar‐chaeal counterparts. Rather than comprising four DNA‐binding domains and a zinc‐finger motif within a single polypeptide of 645 amino acids, as for __Methanococcus jannaschii__, the __Sulfolobus solfataricus__ SSB protein (SsoSSB) has a single DNA‐binding domain in a polypeptide of just 148 amino acids with a eubacterial‐like acidic C‐terminus. SsoSSB protein was purified to homogeneity and found to form tetramers in solution, suggesting a quaternary structure analogous to that of __E. coli__ SSB protein, despite possessing DNA‐binding domains more similar to those of eukaryotic Replication Protein A (RPA). We demonstrate distributive binding of SsoSSB to ssDNA at high temperature with an apparent site size of approximately five nucleotides (nt) per monomer. Additionally, the protein is functional both __in vitro__ and __in vivo__, stimulating RecA protein‐mediated DNA strand‐exchange and rescuing the __ssb‐1__ lethal mutation of __E. coli__ respectively. We dis‐c

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Author

Cynthia A. Haseltine; Stephen C. Kowalczykowski

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0950-382X)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)