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| The EMBO Journal
(2001) 20, 6601–6611, doi:10.1093/emboj/20.23.6601 |
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| Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2 |
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| Simona Ceschini1, Anthony Keeley2, Mark S.B. McAlister3, Mark Oram2, John Phelan3, Laurence H. Pearl1, Irina R. Tsaneva2 and Tracey E. Barrett1 |
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1 Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK 2 Department of Biochemistry and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK 3 Department of Crystallography and BBSRC Bloomsbury Centre for Structural Biology, Birkbeck College, Malet Street, London WC1E 7HX, UK To whom correspondence should be addressed Tracey E. Barrett, barrett@icr.ac.uk Received 6 September 2001; Revised 12 October 2001; Accepted 12 October 2001. |
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| Abstract |
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| Resolution of Holliday junctions into separate DNA duplexes requires enzymatic cleavage of an equivalent strand from each contributing duplex at or close to the point of strand exchange. Diverse Holliday junction-resolving enzymes have been identified in bacteria, bacteriophages, archaea and pox viruses, but the only eukaryotic examples identified so far are those from fungal mitochondria. We have now determined the crystal structure of Ydc2 (also known as SpCce1), a Holliday junction resolvase from the fission yeast Schizosaccharomyces pombe that is involved in the maintenance of mitochondrial DNA. This first structure of a eukaryotic Holliday junction resolvase confirms a distant evolutionary relationship to the bacterial RuvC family, but reveals structural features which are unique to the eukaryotic enzymes. Detailed analysis of the dimeric structure suggests mechanisms for junction isomerization and communication between the two active sites, and together with site-directed mutagenesis identifies residues involved in catalysis. |
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| Keywords: crystal structure, Holliday junction, mitochondrial DNA, resolvase, Schizosaccharomyces pombe |
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