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An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA

Rad54 protein is a key member of the RAD52 epistasis group required for homologous recombination in eukaryotes. Rad54 is a duplex DNA translocase that remodels both DNA and protein–DNA complexes, and functions at multiple steps in the recombination process. Here we use biochemical criteria to demons...

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Detalles Bibliográficos
Autores principales: Haseltine, Cynthia A., Kowalczykowski, Stephen C.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2677860/
https://www.ncbi.nlm.nih.gov/pubmed/19282450
http://dx.doi.org/10.1093/nar/gkp068
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author Haseltine, Cynthia A.
Kowalczykowski, Stephen C.
author_facet Haseltine, Cynthia A.
Kowalczykowski, Stephen C.
author_sort Haseltine, Cynthia A.
collection PubMed
description Rad54 protein is a key member of the RAD52 epistasis group required for homologous recombination in eukaryotes. Rad54 is a duplex DNA translocase that remodels both DNA and protein–DNA complexes, and functions at multiple steps in the recombination process. Here we use biochemical criteria to demonstrate the existence of this important protein in a prokaryotic organism. The Sulfolobus solfataricus Rad54 (SsoRad54) protein is a double-strand DNA-dependent ATPase that can alter the topology of duplex DNA. Like its eukaryotic homolog, it interacts directly with the S. solfataricus Rad51 homologue, SsoRadA, to stimulate DNA strand exchange. Confirmation of this protein as an authentic Rad54 homolog establishes an essential phylogenetic bridge for identifying Rad54 homologs in the archaeal and bacterial domains.
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spelling pubmed-26778602009-05-15 An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA Haseltine, Cynthia A. Kowalczykowski, Stephen C. Nucleic Acids Res Genome Integrity, Repair and Replication Rad54 protein is a key member of the RAD52 epistasis group required for homologous recombination in eukaryotes. Rad54 is a duplex DNA translocase that remodels both DNA and protein–DNA complexes, and functions at multiple steps in the recombination process. Here we use biochemical criteria to demonstrate the existence of this important protein in a prokaryotic organism. The Sulfolobus solfataricus Rad54 (SsoRad54) protein is a double-strand DNA-dependent ATPase that can alter the topology of duplex DNA. Like its eukaryotic homolog, it interacts directly with the S. solfataricus Rad51 homologue, SsoRadA, to stimulate DNA strand exchange. Confirmation of this protein as an authentic Rad54 homolog establishes an essential phylogenetic bridge for identifying Rad54 homologs in the archaeal and bacterial domains. Oxford University Press 2009-05 2009-03-12 /pmc/articles/PMC2677860/ /pubmed/19282450 http://dx.doi.org/10.1093/nar/gkp068 Text en © 2009 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Genome Integrity, Repair and Replication
Haseltine, Cynthia A.
Kowalczykowski, Stephen C.
An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA
title An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA
title_full An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA
title_fullStr An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA
title_full_unstemmed An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA
title_short An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA
title_sort archaeal rad54 protein remodels dna and stimulates dna strand exchange by rada
topic Genome Integrity, Repair and Replication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2677860/
https://www.ncbi.nlm.nih.gov/pubmed/19282450
http://dx.doi.org/10.1093/nar/gkp068
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