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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1992-2-18
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pubmed:abstractText |
The RecD subunit of the RecBCD enzyme from Escherichia coli contains an amino acid sequence common to many enzymes which bind ATP or GTP (Gly-X-X-Gly-X-Gly-Lys-Thr). We have changed the conserved lysine residue (amino acid number 177) in the RecD protein to glutamine to investigate the role of RecD, and ATP-binding to RecD, in the enzymatic activities of RecBCD. The mutant RecD protein assembles with the RecB and RecC subunits and the mutant enzyme, designated RecBCD-K177Q, can be purified in the same way as the wild-type RecBCD enzyme. The mutant RecD subunit in RecBCD-K177Q is photolabeled to a lesser extent by the ATP analogue 8-azido-adenosine-5'-triphosphate than is the wild-type RecD subunit in RecBCD, suggesting that the mutation has reduced the affinity of RecD for ATP.
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pubmed:grant |
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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/8-azidoadenosine 5'-triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Azides,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonuclease V,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/exodeoxyribonuclease V, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
267
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pubmed:geneSymbol |
recD
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1727-32
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1730715-Adenosine Triphosphate,
pubmed-meshheading:1730715-Affinity Labels,
pubmed-meshheading:1730715-Amino Acid Sequence,
pubmed-meshheading:1730715-Azides,
pubmed-meshheading:1730715-Base Sequence,
pubmed-meshheading:1730715-Binding Sites,
pubmed-meshheading:1730715-Escherichia coli,
pubmed-meshheading:1730715-Escherichia coli Proteins,
pubmed-meshheading:1730715-Exodeoxyribonuclease V,
pubmed-meshheading:1730715-Exodeoxyribonucleases,
pubmed-meshheading:1730715-Genes, Bacterial,
pubmed-meshheading:1730715-Kinetics,
pubmed-meshheading:1730715-Lysine,
pubmed-meshheading:1730715-Macromolecular Substances,
pubmed-meshheading:1730715-Molecular Sequence Data,
pubmed-meshheading:1730715-Mutagenesis, Site-Directed,
pubmed-meshheading:1730715-Oligodeoxyribonucleotides,
pubmed-meshheading:1730715-Plasmids,
pubmed-meshheading:1730715-Recombinant Proteins,
pubmed-meshheading:1730715-Restriction Mapping
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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 ATP-binding consensus sequence of the RecD subunit of the Escherichia coli RecBCD enzyme.
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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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