Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2

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 vir...

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Bibliographic Details
Published in:The EMBO journal 2001-12, Vol.20 (23), p.6601-6611
Main Authors: Ceschini, Simona, Keeley, Anthony, McAlister, Mark S.B., Oram, Mark, Phelan, John, Pearl, Laurence H., Tsaneva, Irina R., Barrett, Tracey E.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Catalysis
Catalytic Domain
Cloning, Molecular
crystal structure
Crystallography, X-Ray
Dimerization
Endodeoxyribonucleases - chemistry
Evolution, Molecular
Holliday junction
Isomerism
Mitochondria - enzymology
Mitochondrial DNA
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Open Reading Frames
Protein Binding
Protein Conformation
Protein Folding
Protein Structure, Secondary
resolvase
Schizosaccharomyces - enzymology
Schizosaccharomyces pombe
Schizosaccharomyces pombe Proteins
Sequence Homology, Amino Acid
Ydc2 protein
Yeasts
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Summary: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.
ISSN:0261-4189
1460-2075
1460-2075
DOI:10.1093/emboj/20.23.6601