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PMID: 2253707 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

The accuracy of aminoacylation--ensuring the fidelity of the genetic code.

Experientia ·Vol. 46 ·No. 11-12 ·1990-12-01 ·Pages 1089-96

Söll D

Abstract

The fidelity of protein biosynthesis rests not only on the proper interaction of the messenger RNA codon with the anticodon of the tRNA, but also on the correct attachment of amino acids to their corresponding (cognate) transfer RNA (tRNA) species. This process is catalyzed by the aminoacyl-tRNA synthetases which discriminate with remarkable selectivity amongst many structurally similar tRNAs. The basis for this highly specific recognition of tRNA by these enzymes (also referred to as 'tRNA identity') is currently being elucidated by genetic, biochemical and biophysical techniques. At least two factors are important in determining the accuracy of aminoacylation: a) 'identity elements' in tRNA denote nucleotides in certain positions crucial for protein interactions determining specificity, and b) the occurrence in vivo of competition between synthetases for a particular tRNA which may have ambiguous identity.

MeSH Terms
Amino Acyl-tRNA Synthetases/metabolism,ultrastructure Base Sequence Escherichia coli/genetics,metabolism Genes, Suppressor Genetic Code Molecular Sequence Data Mutation Protein Conformation RNA, Transfer, Gln/genetics,metabolism Structure-Activity Relationship Transfer RNA Aminoacylation
Chemicals
RNA, Transfer, Gln Amino Acyl-tRNA Synthetases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Söll D
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.
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Article Info
Journal
Experientia
Abbr.
Experientia
ISSN
0014-4754
DOI
10.1007/BF01936918
Published
1990-12-01
Pages
1089-96
Language
English
Region
Switzerland
NLM ID
0376547
Subset
IM
External Links
PubMed source DOI: 10.1007/BF01936918
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