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Characterisation of a Holliday junction-resolving enzyme from Schizosaccharomyces pombe

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White_1997_MCB_Characterization.pdf (878.9Kb)
Date
11/1997
Author
White, Malcolm Frederick
Lilley, DMJ
Keywords
Cruciform cutting endonuclease
Saccharomyces-cerevisiae
Escherichia-coli
Mitochondrial-dna
In-vitro
Genetic-recombination
Ruvc resolvase
Resolution
Protein
Yeast
QR Microbiology
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Abstract
The rearrangement and repair of DNA by homologous recombination involves the creation of Holliday junctions, which are cleaved by a class of junction-specific endonucleases to generate recombinant duplex DNA products, Only two cellular junction-resolving enzymes have been identified to date: RuvC in eubacteria and CCE1 from Saccharomyces cerevisiae mitochondria, We have identified a protein from Schizosaccharomyces pombe which has 28% sequence identity to CCE1. The YDC2 protein has been, cloned and overexpressed in Escherichia coli, and the purified recombinant protein has been shown to be a Holliday junction-resolving enzyme. YDC2 has a high degree of specificity for the structure of the four-way junction, to which it binds as a dimer, The enzyme exhibits a sequence specificity for junction cleavage that differs from both CCE1 and RuvC, and it cleaves fixed junctions at the point of strand exchange, The conservation of the mechanism of Holliday junction cleavage between two organisms as diverse as S. cerevisiae and S. pombe suggests that there may be a common pathway for mitochondrial homologous recombination in fungi, plants, protists, and possibly higher eukaryotes.
Citation
White , M F & Lilley , DMJ 1997 , ' Characterisation of a Holliday junction-resolving enzyme from Schizosaccharomyces pombe ' , Molecular and Cellular Biology , vol. 17 , no. 11 , pp. 6465-6471 .
Publication
Molecular and Cellular Biology
Status
Peer reviewed
ISSN
0270-7306
Type
Journal article
Rights
Copyright © 1997, American Society for Microbiology. Open Access article available on Europe PMC.
Description
We thank the Cancer Research Campaign for financial support.
Collections
  • University of St Andrews Research
URL
http://www.scopus.com/inward/record.url?scp=0030857980&partnerID=8YFLogxK
http://europepmc.org/abstract/MED/9343409
http://mcb.asm.org/content/17/11/6465.abstract?sid=f572b001-2195-4c45-a774-236a1b4ba119
URI
http://hdl.handle.net/10023/4953

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