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PMID: 7692438 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

An operational RNA code for amino acids and possible relationship to genetic code.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 19 ·1993-10-01 ·Pages 8763-8

Schimmel P, Giegé R, Moras D, Yokoyama S

Abstract

RNA helical oligonucleotides that recapitulate the acceptor stems of transfer RNAs, and that are devoid of the anticodon trinucleotides of the genetic code, are aminoacylated by aminoacyl tRNA synthetases. The specificity of aminoacylation is sequence dependent, and both specificity and efficiency are generally determined by only a few nucleotides proximal to the amino acid attachment site. This sequence/structure-dependent aminoacylation of RNA oligonucleotides constitutes an operational RNA code for amino acids. To a rough approximation, members of the two different classes of tRNA synthetases are, like tRNAs, organized into two major domains. The class-defining conserved domain containing the active site incorporates determinants for recognition of RNA mini-helix substrates. This domain may reflect the primordial synthetase, which was needed for expression of the operational RNA code. The second synthetase domain, which generally is less or not conserved, provides for interactions with the second domain of tRNA, which incorporates the anticodon. The emergence of the genetic from the operational RNA code could occur when the second domain of synthetases was added with the anticodon-containing domain of tRNAs.

MeSH Terms
Amino Acid Sequence Amino Acids/metabolism Amino Acyl-tRNA Synthetases/metabolism Base Sequence Conserved Sequence Escherichia coli/enzymology,genetics Genetic Code Nucleic Acid Conformation Oligoribonucleotides RNA/genetics RNA, Transfer/genetics,metabolism
Chemicals
Amino Acids Oligoribonucleotides RNA RNA, Transfer Amino Acyl-tRNA Synthetases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schimmel P
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Giegé R
Moras D
Yokoyama S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.19.8763
Published
1993-10-01
Pages
8763-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC47440
Subset
IM
Grants
NIGMS NIH HHS · GM15539 · United States
NIGMS NIH HHS · GM23562 · United States
External Links
PubMed source DOI: 10.1073/pnas.90.19.8763 PMC Full Text View journal details
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