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J. Biol. Chem., Vol. 277, Issue 2, 1553-1559, January 11, 2002
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From the 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
The
-Hairpin Motif of UvrB Is Essential for DNA Binding,
Damage Processing, and UvrC-mediated Incisions*
§,,
Laboratory of Molecular Genetics, NIEHS,
National Institutes of Health, Research Triangle Park, North Carolina
27709, § Department of Molecular Genetics, Cancer Research
Institute, Slovak Academy of Sciences, Vlarska 7, 833 91 Bratislava,
Slovakia, ¶ Department of Pharmacological Sciences, Center for
Structural Biology, State University of New York,
Stony Brook, New York 11794-5115
-hairpin motif
of UvrB might be involved in DNA binding (Theis, K., Chen, P. J.,
Skorvaga, M., Van Houten, B., and Kisker, C. (1999) EMBO J. 18, 6899-6907). To determine a role of the -hairpin of
Bacillus caldotenax UvrB, we have constructed a deletion
mutant, 
h UvrB, which lacks residues Gln-97-Asp-112 of the
-hairpin. h UvrB does not form a stable UvrB-DNA pre-incision
complex and is inactive in UvrABC-mediated incision. However, h
UvrB is able to bind to UvrA and form a complex with UvrA and damaged
DNA, competing with wild type UvrB. In addition, h UvrB shows
wild type-like ATPase activity in complex with UvrA that is stimulated
by damaged DNA. In contrast to wild type UvrB, the ATPase activity of
mutant UvrB does not lead to a destabilization of the damaged duplex.
These results indicate that the conserved -hairpin motif is a major
factor in DNA binding.
*
This research was supported by grants from the Department of
Energy and from the Pew Scholars Program in the Biomedical
Sciences (to C. K.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: NIEHS, P. O. Box
12233, MD D3-01, 111 T. W. Alexander Dr., Research Triangle Park, NC 27709. Tel.: 919-541-2799; E-mail: vanhout1@niehs.nih.gov.
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