Article
- The EMBO Journal (2005) 24, 885 - 894
- doi:10.1038/sj.emboj.7600568
Published online: 3 February 2005
Subject Categories:
Structural insights into the first incision reaction during nucleotide excision repair
James J Truglio1, Benjamin Rhau1, Deborah L Croteau2, Liqun Wang1, Milan Skorvaga2,3, Erkan Karakas1, Matthew J DellaVecchia2, Hong Wang2, Bennett Van Houten2 and Caroline Kisker1
- 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, Research Triangle Park, NC, USA
- Department of Molecular Genetics, Cancer Research Institute, Slovak Academy of Sciences, Bratislava, Slovakia
Correspondence to:
Caroline Kisker, Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, NY 11794-5115, USA. Tel.: +1 631 632 1465; Fax: +1 631 632 1555; E-mail: kisker@pharm.sunysb.edu
Received 3 December 2004; Accepted 7 January 2005
Abstract
Nucleotide excision repair is a highly conserved DNA repair mechanism present in all kingdoms of life. The incision reaction is a critical step for damage removal and is accomplished by the UvrC protein in eubacteria. No structural information is so far available for the 3' incision reaction. Here we report the crystal structure of the N-terminal catalytic domain of UvrC at 1.5 Å resolution, which catalyzes the 3' incision reaction and shares homology with the catalytic domain of the GIY-YIG family of intron-encoded homing endonucleases. The structure reveals a patch of highly conserved residues surrounding a catalytic magnesium-water cluster, suggesting that the metal binding site is an essential feature of UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data strongly suggest that the N-terminal endonuclease domain of UvrC utilizes a novel one-metal mechanism to cleave the phosphodiester bond.
Keywords:
- crystallography,
- DNA damage,
- DNA repair,
- nucleotide excision repair,
- UvrC
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