rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1994-7-7
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pubmed:abstractText |
Through functional studies of mutant tRNAs, we have identified sequence and/or structural features important for specifying the many distinctive properties of E coli initiator tRNA. Many of the mutant tRNAs contain an anticodon sequence change from CAU-->CUA and are now substrates for E coli glutaminyl-tRNA synthetase (GlnRS). We describe here the effect of further mutating the discriminator base 73 and nucleotide 72 at the end of the acceptor stem on: i) recognition of the mutant tRNAs by E coli GlnRS; ii) recognition by E coli methionyl-tRNA transformylase; and iii) activity of the mutant tRNAs in initiation in E coli. For GlnRS recognition, our results are, in general, consistent with interactions found in the crystal structure of the E coli GlnRS-glutamine tRNA complex. The results also support our previous conclusion that formylation of initiator tRNA is important for its function in initiation.
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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/Acyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acyl-tRNA Synthetases,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxymethyl and Formyl...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Met,
http://linkedlifedata.com/resource/pubmed/chemical/glutaminyl-tRNA synthetase,
http://linkedlifedata.com/resource/pubmed/chemical/methionyl-tRNA formyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, formylmethionine-
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pubmed:status |
MEDLINE
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pubmed:issn |
0300-9084
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1051-60
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7515283-Acyltransferases,
pubmed-meshheading:7515283-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:7515283-Base Sequence,
pubmed-meshheading:7515283-Binding Sites,
pubmed-meshheading:7515283-Escherichia coli,
pubmed-meshheading:7515283-Hydroxymethyl and Formyl Transferases,
pubmed-meshheading:7515283-Immunoblotting,
pubmed-meshheading:7515283-Molecular Sequence Data,
pubmed-meshheading:7515283-Mutation,
pubmed-meshheading:7515283-Nucleic Acid Conformation,
pubmed-meshheading:7515283-Peptide Chain Initiation, Translational,
pubmed-meshheading:7515283-RNA, Bacterial,
pubmed-meshheading:7515283-RNA, Transfer, Amino Acyl,
pubmed-meshheading:7515283-RNA, Transfer, Met,
pubmed-meshheading:7515283-Structure-Activity Relationship,
pubmed-meshheading:7515283-Substrate Specificity
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pubmed:year |
1993
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pubmed:articleTitle |
Relationship between the structure and function of Escherichia coli initiator tRNA.
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pubmed:affiliation |
Institute of Cell and Molecular Biology, University of Edinburgh, UK.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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