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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
1993-1-4
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pubmed:abstractText |
The RecB and RecD subunits of the RecBCD enzyme of Escherichia coli contain amino acid sequences similar to a consensus mononucleotide binding motif found in a large number of other enzymes. We have constructed by site-directed mutagenesis a lysine-to-glutamine mutation in this sequence in the RecB protein. The mutant enzyme (RecB-K29Q-CD) has essentially no nuclease or ATP hydrolysis activity on double-stranded DNA, showing the importance of RecB for unwinding double-stranded DNA. However, ATP hydrolysis stimulated by single-stranded DNA is reduced by only about 5-8-fold compared to the wild-type, nuclease activity on single-stranded DNA is reduced by less than 2-fold, and the nuclease activity of the RecB-K29Q-CD enzyme requires ATP. The effects of the RecB mutation suggest that the RecD protein hydrolyzes ATP and can stimulate the RecBCD enzyme nuclease activity on single-stranded DNA.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-1309793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-1310990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-1311326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-1618858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-1730715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-1731253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-1737764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-2069947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-2126155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-2154479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-2476675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-2545239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-2821281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-2841153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-3155726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-3298248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-3534791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-3537960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-3898365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-4263506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-4280072,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-4552016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-4605293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-6295393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-6300771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-6329717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-6337373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-6389498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1454527-942051
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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 |
Nov
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5647-53
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1454527-Adenosine Triphosphatases,
pubmed-meshheading:1454527-Adenosine Triphosphate,
pubmed-meshheading:1454527-Amino Acid Sequence,
pubmed-meshheading:1454527-Base Sequence,
pubmed-meshheading:1454527-Consensus Sequence,
pubmed-meshheading:1454527-Conserved Sequence,
pubmed-meshheading:1454527-DNA, Bacterial,
pubmed-meshheading:1454527-Escherichia coli,
pubmed-meshheading:1454527-Escherichia coli Proteins,
pubmed-meshheading:1454527-Exodeoxyribonuclease V,
pubmed-meshheading:1454527-Exodeoxyribonucleases,
pubmed-meshheading:1454527-Hydrolysis,
pubmed-meshheading:1454527-Kinetics,
pubmed-meshheading:1454527-Lysine,
pubmed-meshheading:1454527-Molecular Sequence Data,
pubmed-meshheading:1454527-Mutagenesis, Site-Directed
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pubmed:year |
1992
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pubmed:articleTitle |
Alteration by site-directed mutagenesis of the conserved lysine residue in the consensus ATP-binding sequence of the RecB protein of Escherichia coli.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Maryland, College Park 20742.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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