PMID:11687584
| Citation |
Skorvaga, M, Theis, K, Mandavilli, BS, Kisker, C and Van Houten, B (2002) The beta -hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions. J. Biol. Chem. 277:1553-9 |
|---|---|
| Abstract |
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 (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 beta-hairpin of Bacillus caldotenax UvrB, we have constructed a deletion mutant, Deltabetah UvrB, which lacks residues Gln-97-Asp-112 of the beta-hairpin. Deltabetah UvrB does not form a stable UvrB-DNA pre-incision complex and is inactive in UvrABC-mediated incision. However, Deltabetah UvrB is able to bind to UvrA and form a complex with UvrA and damaged DNA, competing with wild type UvrB. In addition, Deltabetah 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 beta-hairpin motif is a major factor in DNA binding. |
| Links |
PubMed Online version:10.1074/jbc.M108847200 |
| Keywords |
Adenosine Triphosphatases/metabolism; Amino Acid Motifs; Bacillus/metabolism; Bacterial Proteins/metabolism; Circular Dichroism; DNA/metabolism; DNA Helicases/chemistry; DNA Helicases/genetics; DNA Helicases/metabolism; DNA Repair; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Endodeoxyribonucleases/metabolism; Escherichia coli Proteins; Molecular Structure; Protein Structure, Secondary; Protein Subunits |
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