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Papers In Press, published online ahead of print October 30, 2001
Laboratory of Molecular Genetics, NIEHS, Research Triangle Park, NC 27709
Corresponding Author: vanhout1{at}niehs.nih.gov
UvrB plays a major role in recognition and processing of DNA lesions during nucleotide excision repair. The crystal structure of UvrB revealed a similar fold as found in monomeric DNA helicases. Homology modeling suggested that the beta-hairpin motif of UvrB might be involved in DNA binding (EMBOJ 18:6899-6907, 1999). To determine a role of the beta-hairpin of Bacillus caldotenax UvrB, we have constructed a deletion mutant, Dbh UvrB, which lacks residues Q97-D112 of the b-hairpin. Dbh UvrB does not form a stable UvrB-DNA pre-incision complex and is inactive in UvrABC-mediated incision. However, Dbh UvrB is able to bind to UvrA and form a complex with UvrA, and damaged DNA, competing with wild type UvrB. In addition, Dbh UvrB shows wild type-like ATPase activity in complex with UvrA that is stimulated by damaged DNA. In contrast to wt UvrB, the ATPase activity of mutant UvrB does not lead to a destabilization of the damaged duplex. These results indicate that the conserved beta-hairpin motif is a major factor in DNA binding.
J. Biol. Chem, 10.1074/jbc.M108847200
Submitted on September 13, 2001
Revised on October 24, 2001
Accepted on October 26, 2001
Beta-hairpin motif of UvrB is essential for DNA binding, damage processing and UvrC mediated-incisions
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