Selection of suppressor methionyl-tRNA synthetases: mapping the tRNA anticodon binding site. 1991

T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
Laboratoire de Biochimie, Unité Associée 240 du Centre National de la Recherche Scientifique, Ecole Polytechnique, Palaiseau, France.

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.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008718 Methionine-tRNA Ligase An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10. Methionyl T RNA Synthetase,Met-tRNA Ligase,Methionyl-tRNA Synthetase,Ligase, Met-tRNA,Ligase, Methionine-tRNA,Met tRNA Ligase,Methionine tRNA Ligase,Methionyl tRNA Synthetase,Synthetase, Methionyl-tRNA
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D000926 Anticodon The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome. Anticodons
D012343 RNA, Transfer The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains. Suppressor Transfer RNA,Transfer RNA,tRNA,RNA, Transfer, Suppressor,Transfer RNA, Suppressor,RNA, Suppressor Transfer
D013489 Suppression, Genetic Mutation process that restores the wild-type PHENOTYPE in an organism possessing a mutationally altered GENOTYPE. The second "suppressor" mutation may be on a different gene, on the same gene but located at a distance from the site of the primary mutation, or in extrachromosomal genes (EXTRACHROMOSOMAL INHERITANCE). Suppressor Mutation,Genetic Suppression,Genetic Suppressions,Mutation, Suppressor,Mutations, Suppressor,Suppressions, Genetic,Suppressor Mutations
D014644 Genetic Variation Genotypic differences observed among individuals in a population. Genetic Diversity,Variation, Genetic,Diversity, Genetic,Diversities, Genetic,Genetic Diversities,Genetic Variations,Variations, Genetic
D016297 Mutagenesis, Site-Directed Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion. Mutagenesis, Oligonucleotide-Directed,Mutagenesis, Site-Specific,Oligonucleotide-Directed Mutagenesis,Site-Directed Mutagenesis,Site-Specific Mutagenesis,Mutageneses, Oligonucleotide-Directed,Mutageneses, Site-Directed,Mutageneses, Site-Specific,Mutagenesis, Oligonucleotide Directed,Mutagenesis, Site Directed,Mutagenesis, Site Specific,Oligonucleotide Directed Mutagenesis,Oligonucleotide-Directed Mutageneses,Site Directed Mutagenesis,Site Specific Mutagenesis,Site-Directed Mutageneses,Site-Specific Mutageneses

Related Publications

T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
March 1990, Biochemistry,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
October 1993, Biochemistry,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
January 1986, Biochemistry,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
August 1990, Biochimie,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
May 2013, Trends in biochemical sciences,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
April 1999, The Biochemical journal,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
April 2003, The EMBO journal,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
January 1983, Molekuliarnaia biologiia,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
December 2004, Journal of molecular biology,
T Meinnel, and Y Mechulam, and D Le Corre, and M Panvert, and S Blanquet, and G Fayat
April 1991, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!