Compilation of mutant suppressor tRNA sequences
Julio E. Celis,Peter W. Piper +1 more
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This article is published in Nucleic Acids Research.The article was published on 1982-01-22 and is currently open access. It has received 21 citations till now. The article focuses on the topics: Mutant & Mutation (genetic algorithm).read more
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Transfer ribonucleic acid-mediated suppression of termination codons in Escherichia coli.
Gudmundur Eggertsson,Dieter Söll +1 more
Journal ArticleDOI
Role of the extra G-C pair at the end of the acceptor stem of tRNA(His) in aminoacylation.
Hyouta Himeno,Tsunemi Hasegawa,Takuya Ueda,Kimitsuna Watanabe,Kin-ichiro Miura,Mikio Shimizu +5 more
TL;DR: In vitro transcripts constructed demonstrate that the set of the G-1-C73 pair at the end of the acceptor stem of histidine tRNA is crucial for the catalytic process of aminoacylation.
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Use of supF, an Escherichia coli tyrosine suppressor tRNA gene, as a mutagenic target in shuttle-vector plasmids.
TL;DR: The supF gene is thus an extremely sensitive target for mutagenic inactivation in shuttle-vector plasmids, and single or tandem base-substitution mutations that reduce or eliminate suppressor activity were identified.
Journal ArticleDOI
A complex profile of protein elongation: translating chemical energy into molecular movement
Kenton Abel,Frances Jurnak +1 more
TL;DR: The recently solved structures of the protein elongation factor complexes, EF-Tu-GDPNP-phenylalanyl-tRNA and EF-T-Ts, complete the atomic profile of four EF- Tu conformational states and suggest an atomic model for movement duringprotein elongation and, by molecular mimicry with EF-G, translocation as well.
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Recognition of tRNATyr by tyrosyl-tRNA synthetase
TL;DR: The results of in vivo genetic complementation experiments indicate that the identity elements of tRNAs and the recognition mechanisms of such elements by the synthetases have been conserved during evolution.