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Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2.
6601 - 6611.
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.
|Title:||Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2|
|Keywords:||crystal structure, Holliday junction, mitochondrial DNA, resolvase, Schizosaccharomyces pombe, 4-WAY DNA JUNCTION, SCHIZOSACCHAROMYCES-POMBE, ESCHERICHIA-COLI, ENZYME CCE1, SACCHAROMYCES-CEREVISIAE, GENETIC-RECOMBINATION, SEQUENCE SPECIFICITY, ENDONUCLEASE CCE1, BRANCH MIGRATION, RUVC RESOLVASE|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology|
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