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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2009-10-19
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pubmed:abstractText |
During nucleotide excision repair (NER) in bacteria the UvrC nuclease and the short oligonucleotide that contains the DNA lesion are removed from the post-incision complex by UvrD, a superfamily 1A helicase. Helicases are frequently regulated by interactions with partner proteins, and immunoprecipitation experiments have previously indicated that UvrD interacts with UvrB, a component of the post-incision complex. We examined this interaction using 2-hybrid analysis and surface plasmon resonance spectroscopy, and found that the N-terminal domain and the unstructured region at the C-terminus of UvrD interact with UvrB. We analysed the properties of a truncated UvrD protein that lacked the unstructured C-terminal region and found that it showed a diminished affinity for single-stranded DNA, but retained the ability to displace both UvrC and the lesion-containing oligonucleotide from a post-incision nucleotide excision repair complex. The interaction of the C-terminal region of UvrD with UvrB is therefore not an essential feature of the mechanism by which UvrD disassembles the post-incision complex during NER. In further experiments we showed that PcrA helicase from Bacillus stearothermophilus can also displace UvrC and the excised oligonucleotide from a post-incision NER complex, which supports the idea that PcrA performs a UvrD-like function during NER in gram-positive organisms.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-10198018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-10212225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-10518516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-10543970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-10601012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-10829079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-11101153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-11914359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-15192705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-1530937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-15952900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-16464004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-16532007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-16935885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-17190599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-17376770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-17870087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-19208629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-19317511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-2931721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-2987825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-3161077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-4879097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-7713940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-8087855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-9121589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-9482750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-9499408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-9512562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-9580688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-9592155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19762288-9701819
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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,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/UvrA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/UvrB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/UvrD protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1568-7856
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
2
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1300-10
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pubmed:dateRevised |
2011-7-20
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pubmed:meshHeading |
pubmed-meshheading:19762288-Adenosine Triphosphatases,
pubmed-meshheading:19762288-DNA,
pubmed-meshheading:19762288-DNA Helicases,
pubmed-meshheading:19762288-DNA Repair,
pubmed-meshheading:19762288-DNA-Binding Proteins,
pubmed-meshheading:19762288-Escherichia coli,
pubmed-meshheading:19762288-Escherichia coli Proteins,
pubmed-meshheading:19762288-Models, Molecular,
pubmed-meshheading:19762288-Nucleic Acid Conformation,
pubmed-meshheading:19762288-Protein Binding,
pubmed-meshheading:19762288-Protein Structure, Tertiary,
pubmed-meshheading:19762288-Substrate Specificity
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pubmed:year |
2009
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pubmed:articleTitle |
The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair.
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pubmed:affiliation |
DNA-protein Interactions Unit, Department of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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