| Literature DB >> 27519413 |
Stefanie H Chen1, Rose T Byrne-Nash2, Michael M Cox2.
Abstract
The bacterial single-stranded DNA binding protein (SSB) acts as an organizer of DNA repair complexes. The radD gene was recently identified as having an unspecified role in repair of radiation damage and, more specifically, DNA double-strand breaks. Purified RadD protein displays a DNA-independent ATPase activity. However, ATP hydrolytic rates are stimulated by SSB through its C terminus. The RadD and SSB proteins also directly interact in vivo in a yeast two-hybrid assay and in vitro through ammonium sulfate co-precipitation. Therefore, it is likely that the repair function of RadD is mediated through interaction with SSB at the site of damage.Entities:
Keywords: ATPase; DNA repair; SSB; helicase; protein-DNA interaction; protein-protein interaction; radiation biology
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Year: 2016 PMID: 27519413 PMCID: PMC5034066 DOI: 10.1074/jbc.M116.736223
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157