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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0043393,
umls-concept:C0205369,
umls-concept:C0684321,
umls-concept:C1148735,
umls-concept:C1158558,
umls-concept:C1167117,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636
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pubmed:issue |
1
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pubmed:dateCreated |
2007-10-15
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pubmed:abstractText |
Lesions in the template DNA strand block the progression of the replication fork. In the yeast Saccharomyces cerevisiae, replication through DNA lesions is mediated by different Rad6-Rad18-dependent means, which include translesion synthesis and a Rad5-dependent postreplicational repair pathway that repairs the discontinuities that form in the DNA synthesized from damaged templates. Although translesion synthesis is well characterized, little is known about the mechanisms that modulate Rad5-dependent postreplicational repair. Here we show that yeast Rad5 has a DNA helicase activity that is specialized for replication fork regression. On model replication fork structures, Rad5 concertedly unwinds and anneals the nascent and the parental strands without exposing extended single-stranded regions. These observations provide insight into the mechanism of postreplicational repair in which Rad5 action promotes template switching for error-free damage bypass.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-10089880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-10373362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-10871364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-10880451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-11433031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-11545742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-11884624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-12142537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-12226657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-1255724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-12764199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-12837266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-1324406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-15121847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-15629726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-15952890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-16247017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-16387650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-16766518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-16908531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-17003056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-17108083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-17115688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-17130289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-17964257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-7737132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-7926769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-7961763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-8618826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-8658138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-8790390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-9153257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-9287349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-9637242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17936713-9974380
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
167-75
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2007
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pubmed:articleTitle |
Yeast Rad5 protein required for postreplication repair has a DNA helicase activity specific for replication fork regression.
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pubmed:affiliation |
Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Temesvari krt.62, H-6726, Hungary.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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