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PMID: 10481006 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Recognition of the codon-anticodon helix by ribosomal RNA.

Science (New York, N.Y.) ·Vol. 285 ·No. 5434 ·1999-09-10 ·Pages 1722-5

Yoshizawa S, Fourmy D, Puglisi JD

Abstract

Translational fidelity is established by ribosomal recognition of the codon-anticodon interaction within the aminoacyl-transfer RNA (tRNA) site (A site) of the ribosome. Experiments are presented that reveal possible contacts between 16S ribosomal RNA and the codon-anticodon complex. N1 methylation of adenine at position 1492 (A1492) and A1493 interfered with A-site tRNA binding. Mutation of A1492 and A1493 to guanine or cytosine also impaired A-site tRNA binding. The deleterious effects of A1492G or A1493G (or both) mutations were compensated by 2'fluorine substitutions in the mRNA codon. The results suggest that the ribosome recognizes the codon-anticodon complex by adenine contacts to the messenger RNA backbone and provide a mechanism for molecular discrimination of correct versus incorrect codon-anticodon pairs.

MeSH Terms
Adenine/analogs & derivatives,metabolism Anticodon/chemistry,metabolism Binding Sites Biotin Codon/chemistry,metabolism Escherichia coli Hydrogen Bonding Methylation Mutagenesis, Site-Directed Nucleic Acid Conformation Paromomycin/pharmacology Protein Biosynthesis RNA, Bacterial/chemistry,metabolism RNA, Ribosomal, 16S/chemistry,genetics,metabolism RNA, Transfer, Met/metabolism RNA, Transfer, Phe/metabolism Ribosomes/metabolism
Chemicals
Anticodon Codon RNA, Bacterial RNA, Ribosomal, 16S RNA, Transfer, Met RNA, Transfer, Phe tRNA, formylmethionine- 1-methyladenine Paromomycin Biotin Adenine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Yoshizawa S
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.
Fourmy D
Puglisi J D
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1999-09-10
Pages
1722-5
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIGMS NIH HHS · GM51266 · United States
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