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PMID: 3045821 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 85 ·No. 18 ·1988-09-00 ·Pages 6627-31

Rogers MJ, Söll D

Abstract

Analysis of the in vivo amber suppressor activity of mutants derived from two Escherichia coli serine tRNAs shows that substitution of 2 base pairs in the acceptor helix changes a serine suppressor tRNA to an efficient glutamine acceptor. Determination of the amino acid inserted in vivo into protein by this tRNA shows that these changes reduce the tRNA recognition by seryl-tRNA synthetase while increasing that of glutaminyl-tRNA synthetase. This implies that misaminoacylation in vivo is dependent on the competition by different synthetases for the tRNA. In addition, the "translational efficiency" of tRNA is an integral part in observing misaminoacylation in vivo.

MeSH Terms
Amino Acyl-tRNA Synthetases/metabolism Codon Escherichia coli/genetics Glutamate-tRNA Ligase/metabolism Glutamine/metabolism Mutation Nucleic Acid Conformation Protein Biosynthesis RNA, Transfer, Glu/biosynthesis RNA, Transfer, Ser/biosynthesis Repressor Proteins/genetics Serine-tRNA Ligase/metabolism Substrate Specificity
Chemicals
Codon RNA, Transfer, Glu RNA, Transfer, Ser Repressor Proteins Glutamine Amino Acyl-tRNA Synthetases Serine-tRNA Ligase Glutamate-tRNA Ligase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Rogers M J
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Söll D
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34 references, click to expand
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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.85.18.6627
Published
1988-09-00
Pages
6627-31
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC282030
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.85.18.6627 PMC Full Text View journal details
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