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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1989-10-26
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pubmed:abstractText |
Eucaryotic initiation factor 4A (eIF-4A) is a member of a family of proteins believed to be involved in the ATP-dependent melting of RNA secondary structure. These proteins contain a derivative of the consensus ATP-binding site AXXGXGKT. To assess the importance of the consensus amino acid sequence in eIF-4A for ATP binding, we mutated the consensus amino-proximal glycine and lysine to isoleucine and asparagine, respectively. The effect of the mutations was examined by UV-induced cross-linking of [alpha-32P]dATP to eIF-4A. Mutation of the lysine residue (but not of the glycine residue) resulted in the loss of [alpha-32P]dATP cross-linking to eIF-4A, suggesting that the lysine is an important determinant in ATP binding to eIF-4A.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-2451786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-2461520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-2535893,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-2563148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-2648398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-2720782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-2869483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-3046931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-3052853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-3140040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-3537305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-3838990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-3840589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-4055759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-592399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-6145716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-6329717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-641056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-6604056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2506440-6757864
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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 |
Sep
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4061-3
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2506440-Adenosine Triphosphate,
pubmed-meshheading:2506440-Amino Acid Sequence,
pubmed-meshheading:2506440-Animals,
pubmed-meshheading:2506440-Binding Sites,
pubmed-meshheading:2506440-Eukaryotic Initiation Factor-4A,
pubmed-meshheading:2506440-Lysine,
pubmed-meshheading:2506440-Mice,
pubmed-meshheading:2506440-Molecular Sequence Data,
pubmed-meshheading:2506440-Mutation,
pubmed-meshheading:2506440-Nucleotides,
pubmed-meshheading:2506440-Peptide Initiation Factors
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pubmed:year |
1989
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pubmed:articleTitle |
A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity.
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pubmed:affiliation |
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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