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PMID: 1986377 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Selection of suppressor methionyl-tRNA synthetases: mapping the tRNA anticodon binding site.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 1 ·1991-01-01 ·Pages 291-5

Meinnel T, Mechulam Y, Le Corre D, Panvert M, Blanquet S, Fayat G

Abstract

Accurate aminoacylation of a tRNA by Escherichia coli methionyl-tRNA synthetase (MTS) is specified by the CAU anticodon. A genetic screening procedure was designed to isolate MTS mutants able to aminoacylate a methionine amber tRNA (CUA anticodon). Selected suppressor MTS enzymes all possess one or several mutations in the vicinity of Trp-461, a residue that is the major contributor to the stability of complexes formed with tRNAs having the cognate CAU anticodon. Analysis of catalytic properties of purified suppressor enzymes shows that they have acquired an additional specificity toward the amber anticodon without complete disruption of the methionine anticodon site. It is concluded that both positive and negative discrimination toward the binding of tRNA anticodon sequences is restricted to a limited region of the synthetase, residues 451-467.

MeSH Terms
Anticodon/genetics,metabolism Escherichia coli/enzymology,genetics Genes, Bacterial Genetic Variation Kinetics Methionine-tRNA Ligase/genetics,metabolism Mutagenesis, Site-Directed RNA, Transfer/genetics,isolation & purification,metabolism Suppression, Genetic
Chemicals
Anticodon RNA, Transfer Methionine-tRNA Ligase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Meinnel T
Laboratoire de Biochimie, Unité Associée 240 du Centre National de la Recherche Scientifique, Ecole Polytechnique, Palaiseau, France.
Mechulam Y
Le Corre D
Panvert M
Blanquet S
Fayat G
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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.88.1.291
Published
1991-01-01
Pages
291-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC50796
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.88.1.291 PMC Full Text View journal details
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