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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1992-5-13
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pubmed:abstractText |
This paper focuses on several aspects of the specificity of mutants of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) and tRNA(Gln). Temperature-sensitive mutants located in glnS, the gene for GlnRS, have been described previously. The mutations responsible for the temperature-sensitive phenotype were analyzed, and pseudorevertants of these mutants isolated and characterized. The nature of these mutations is discussed in terms of their location in the three-dimensional structure of the tRNA(Gln).GlnRS complex. In order to characterize the specificity of the aminoacylation reaction, mutant tRNA(Gln) species were synthesized with either a 2'-deoxy AMP or 3'-deoxy AMP as their 3'-terminal nucleotide. Subsequent assays for aminoacylation and ATP/PPi exchange activity established the esterification of glutamine to the 2'-hydroxyl of the terminal adenosine; there is no glutaminylation of the 3'-OH group. This correlates with the classification of GlnRS as a class I aminoacyl-tRNA synthetase. Mutations in tRNA(Gln) are discussed which affect the recognition of GlnRS and the current concept of glutamine identity in E coli is reviewed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0300-9084
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
73
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pubmed:geneSymbol |
glnS
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1501-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1725262-Base Sequence,
pubmed-meshheading:1725262-Binding Sites,
pubmed-meshheading:1725262-Escherichia coli,
pubmed-meshheading:1725262-Gene Expression Regulation, Bacterial,
pubmed-meshheading:1725262-Glutamate-tRNA Ligase,
pubmed-meshheading:1725262-Molecular Sequence Data,
pubmed-meshheading:1725262-Mutation,
pubmed-meshheading:1725262-Nucleic Acid Conformation,
pubmed-meshheading:1725262-RNA, Bacterial,
pubmed-meshheading:1725262-RNA, Transfer, Gln,
pubmed-meshheading:1725262-Temperature
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pubmed:year |
1991
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pubmed:articleTitle |
Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNA(Gln) interaction.
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pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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