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PMID: 16260144 Published · ppublish English Journal Article Research Support, N.I.H., Extramural

Amino acid specificity in translation.

Trends in biochemical sciences ·Vol. 30 ·No. 12 ·2005-12-00 ·Pages 659-65

Dale T, Uhlenbeck OC

Abstract

Recent structural and biochemical experiments indicate that bacterial elongation factor Tu and the ribosomal A-site show specificity for both the amino acid and the tRNA portions of their aminoacyl-tRNA (aa-tRNA) substrates. These data are inconsistent with the traditional view that tRNAs are generic adaptors in translation. We hypothesize that each tRNA sequence has co-evolved with its cognate amino acid, such that all aa-tRNAs are translated uniformly.

MeSH Terms
Amino Acids/genetics,metabolism Amino Acyl-tRNA Synthetases/chemistry,genetics,metabolism Binding Sites Models, Biological Models, Molecular Peptide Elongation Factor Tu/chemistry,genetics,metabolism Protein Biosynthesis RNA, Transfer, Amino Acyl/chemistry,genetics,metabolism Ribosomes/metabolism Thermodynamics
Chemicals
Amino Acids RNA, Transfer, Amino Acyl Peptide Elongation Factor Tu Amino Acyl-tRNA Synthetases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Dale Taraka
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
Uhlenbeck Olke C
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
2005-12-00
Epub
2005-00-02
Pages
659-65
Language
English
Region
England
NLM ID
7610674
Subset
IM
Grants
NIGMS NIH HHS · GM37552 · United States
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