Literature DB >> 3525546

The translational efficiency of tRNA is a property of the anticodon arm.

M Yarus, S Cline, L Raftery, P Wier, D Bradley.   

Abstract

We have reciprocally transplanted the anticodon arm sequences of a set of amber suppressor tRNA genes, using recombinant DNA techniques. By this means, a very efficient suppressor may be converted to a poor one, and the poorest tRNA to the efficiency of the best one. In tRNA molecules of normal 2 degrees and 3 degrees structure, the suppressor efficiencies of different composite tRNAs having the same anticodon arm sequence are approximately the same. Large numbers of simultaneous changes throughout the rest of the molecule do not affect the efficiency. Selective nucleotide modification as a result of varied anticodon arm sequences cannot explain these efficiencies. Efficiencies are also unlikely to differ because of selective aminoacylation. Measurement of in vivo tRNA shows, however, that tRNA levels do vary if the anticodon arm sequence is changed. If tRNA levels are normalized, the anticodon arm effect on the translational efficiency remains. Therefore, different anticodon arms, all of normal secondary structure, are not equivalent in translation. The most efficient sequences in this series resemble those found in natural tRNAs associated with similar anticodons, as is proposed in the extended anticodon theory (Yarus, M. (1982) Science 218, 646-652). These molecules also provide some information on the specificity of nucleotide modification enzymes and on determinants of the steady-state tRNA level.

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Year:  1986        PMID: 3525546

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  19 in total

1.  Structural alterations of the tRNA(m1G37)methyltransferase from Salmonella typhimurium affect tRNA substrate specificity.

Authors:  J N Li; G R Björk
Journal:  RNA       Date:  1999-03       Impact factor: 4.942

2.  Mutations which alter the elbow region of tRNA2Gly reduce T4 gene 60 translational bypassing efficiency.

Authors:  A J Herr; J F Atkins; R F Gesteland
Journal:  EMBO J       Date:  1999-05-17       Impact factor: 11.598

3.  Analysis of genomic tRNA sets from Bacteria, Archaea, and Eukarya points to anticodon-codon hydrogen bonds as a major determinant of tRNA compositional variations.

Authors:  Ilia Targanski; Vera Cherkasova
Journal:  RNA       Date:  2008-04-25       Impact factor: 4.942

4.  Discrimination between glutaminyl-tRNA synthetase and seryl-tRNA synthetase involves nucleotides in the acceptor helix of tRNA.

Authors:  M J Rogers; D Söll
Journal:  Proc Natl Acad Sci U S A       Date:  1988-09       Impact factor: 11.205

Review 5.  Transfer ribonucleic acid-mediated suppression of termination codons in Escherichia coli.

Authors:  G Eggertsson; D Söll
Journal:  Microbiol Rev       Date:  1988-09

Review 6.  Errors and alternatives in reading the universal genetic code.

Authors:  J Parker
Journal:  Microbiol Rev       Date:  1989-09

7.  The bases of the tRNA anticodon loop are independent by genetic criteria.

Authors:  D Smith; L Breeden; E Farrell; M Yarus
Journal:  Nucleic Acids Res       Date:  1987-06-11       Impact factor: 16.971

8.  Complete set of orthogonal 21st aminoacyl-tRNA synthetase-amber, ochre and opal suppressor tRNA pairs: concomitant suppression of three different termination codons in an mRNA in mammalian cells.

Authors:  Caroline Köhrer; Eric L Sullivan; Uttam L RajBhandary
Journal:  Nucleic Acids Res       Date:  2004-12-01       Impact factor: 16.971

9.  Nonsense suppression in archaea.

Authors:  Arpita Bhattacharya; Caroline Köhrer; Debabrata Mandal; Uttam L RajBhandary
Journal:  Proc Natl Acad Sci U S A       Date:  2015-04-27       Impact factor: 11.205

10.  A sequence element that tunes Escherichia coli tRNA(Ala)(GGC) to ensure accurate decoding.

Authors:  Sarah Ledoux; Mikołaj Olejniczak; Olke C Uhlenbeck
Journal:  Nat Struct Mol Biol       Date:  2009-03-22       Impact factor: 15.369

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