Escherichia coli RadD Protein Functionally Interacts with the Single-stranded DNA-binding Protein*
- ↵1 To whom correspondence should be addressed: Dept. of Biochemistry, University of Wisconsin-Madison, 433 Babcock Dr., Rm. 337, Madison, WI 53706. Tel.: 608-262-7982; Fax: 608-265-2603; E-mail: slchen3{at}wisc.edu.
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.
- ATPase
- DNA repair
- protein-DNA interaction
- protein-protein interaction
- radiation biology
- SSB
- helicase
Footnotes
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↵* This work was supported in whole or part by the National Institutes of Health Grant GM032335 (to M. M. C.). The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
- Received May 3, 2016.
- Revision received August 3, 2016.
- © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
