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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2004-10-1
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pubmed:abstractText |
Replication forks arrested by inactivation of the main Escherichia coli DNA polymerase (polymerase III) are reversed by the annealing of newly synthesized leading- and lagging-strand ends. Reversed forks are reset by the action of RecBC on the DNA double-strand end, and in the absence of RecBC chromosomes are linearized by the Holliday junction resolvase RuvABC. We report here that the UvrD helicase is essential for RuvABC-dependent chromosome linearization in E. coli polymerase III mutants, whereas its partners in DNA repair (UvrA/B and MutL/S) are not. We conclude that UvrD participates in replication fork reversal in E. coli.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-10585965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-10600744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-10632890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-10754552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-10835635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-10984488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-10990466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-11069680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-11157768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-11459951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-11879732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-11994158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-12028381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-12142524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-12142525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-12748189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-1849510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-2166955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-2543977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-2665076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-2942537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-350859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-6125389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-7651328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-8289272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-8335623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-8341594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-8419285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-9228029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-9393722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-9402025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-9442895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-9535911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15375374-9814711
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase III,
http://linkedlifedata.com/resource/pubmed/chemical/DNA polymerase III, alpha subunit,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonuclease V,
http://linkedlifedata.com/resource/pubmed/chemical/UvrD protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/beta subunit, DNA polymerase III,
http://linkedlifedata.com/resource/pubmed/chemical/exodeoxyribonuclease V, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1469-221X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
983-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2004
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pubmed:articleTitle |
The DNA repair helicase UvrD is essential for replication fork reversal in replication mutants.
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pubmed:affiliation |
Laboratoire de Génétique Microbienne, Institut National de la Recherche Agronomique, 78352 Jouy en Josas, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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