Article
- The EMBO Journal (2007) 26, 613 - 622
- doi:10.1038/sj.emboj.7601497
Subject Categories:
Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad
Erkan Karakas1,a, James J Truglio1,a, Deborah Croteau2, Benjamin Rhau1, Liqun Wang1, Bennett Van Houten2 and Caroline Kisker1,3
- Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, NY, USA
- Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, National Institutes of Health, NC, USA
- Rudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, Würzburg, Germany
Correspondence to:
Caroline Kisker, Rudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, Versbacher Strasse 9, 97078 Würzburg, Germany. Tel.: +49 931 201 48300; Fax: +49 931 201 48309; E-mail: caroline.kisker@virchow.uni-wuerzburg.de
aThese authors contributed equally to this work
Received 4 August 2006; Accepted 15 November 2006
Abstract
Removal and repair of DNA damage by the nucleotide excision repair pathway requires two sequential incision reactions, which are achieved by the endonuclease UvrC in eubacteria. Here, we describe the crystal structure of the C-terminal half of UvrC, which contains the catalytic domain responsible for 5' incision and a helix–hairpin–helix–domain that is implicated in DNA binding. Surprisingly, the 5' catalytic domain shares structural homology with RNase H despite the lack of sequence homology and contains an uncommon DDH triad. The structure also reveals two highly conserved patches on the surface of the protein, which are not related to the active site. Mutations of residues in one of these patches led to the inability of the enzyme to bind DNA and severely compromised both incision reactions. Based on our results, we suggest a model of how UvrC forms a productive protein–DNA complex to excise the damage from DNA.
Keywords:
- DNA damage,
- DNA repair,
- endonuclease,
- nucleotide excision repair,
- UvrC,
- RNase H
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