PMID:1725262
| Citation |
Englisch-Peters, S, Conley, J, Plumbridge, J, Leptak, C, Söll, D and Rogers, MJ (1991) Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNA(Gln) interaction. Biochimie 73:1501-8 |
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| Abstract |
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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| Keywords |
Base Sequence; Binding Sites; Escherichia coli/genetics; Gene Expression Regulation, Bacterial; Glutamate-tRNA Ligase/genetics; Glutamate-tRNA Ligase/metabolism; Molecular Sequence Data; Mutation; Nucleic Acid Conformation; RNA, Bacterial/genetics; RNA, Bacterial/metabolism; RNA, Transfer, Gln/chemistry; RNA, Transfer, Gln/genetics; RNA, Transfer, Gln/metabolism; Temperature |
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