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Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.
- P. Hirel, M. Schmitter, P. Dessen, G. Fayat, S. Blanquet
- BiologyProceedings of the National Academy of Sciences…
- 1 November 1989
From the results, methionine excision catalyzed by MAP is shown to obey the following rule: the catalytic efficiency of MAP, and therefore the extent of cleavage, decreases in parallel with the increasing of the maximal side-chain length of the amino acid in the penultimate position.
Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction.
Sets of parameters governing the rules were determined under various mutagenic conditions including the addition of MnCl2 and validity of the rules was assessed in several mutagenesis experiments showing that a wide range of substitution frequencies including AT-->GC and GC-->AT transitions as well as AT-->TA transversions can be obtained at will.
Sequence of a 1.26‐kb DNA fragment containing the structural gene for E.coli initiation factor IF3: presence of an AUU initiator codon.
The nucleotide sequence of a 1.26‐kb pair DNA fragment containing the structural gene for Escherichia coli initiation factor IF3 has been determined and the presence of AUU as the translational initiator codon is determined.
Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl‐tRNA hydrolase
- E. Schmitt, Y. Mechulam, M. Fromant, P. Plateau, S. Blanquet
- Biology, ChemistryThe EMBO journal
- 1 August 1997
The structure of crystalline peptidyl‐tRNA hydrolase could be solved at 1.2 Å resolution and indicates a single α/β globular domain built around a twisted mixed β‐sheet, similar to the central core of an aminopeptidase from Aeromonas proteolytica.
Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli
- J. Guillon, Y. Mechulam, J. Schmitter, S. Blanquet, G. Fayat
- BiologyJournal of bacteriology
- 1 July 1992
In bacteria, as well as in chloroplasts and mitochondria, the free amino group of the methionylated initiator tRNA(fMet) is specifically modified by the addition of a formyl group. The importance of…
Extracellular Production of Hydrogen Selenide Accounts for Thiol-assisted Toxicity of Selenite against Saccharomyces cerevisiae*
It is shown that the lethal dose of selenite is reduced to the micromolar range by the presence of thiols in the growth medium, and the possibility that selenium exerts its toxicity through consumption of intracellular reduced glutathione, thus leading to severe oxidative stress is discussed.
Structural Basis of RNA-Dependent Recruitment of Glutamine to the Genetic Code
Glutaminyl–transfer RNA (Gln-tRNAGln) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNAGln by the heterodimeric Glu-tRNAGln amidotransferase GatDE. Here we report the…
Structural basis for tRNA-dependent amidotransferase function.
Metabolism of d-Aminoacyl-tRNAs inEscherichia coli and Saccharomyces cerevisiae Cells*
- J. Soutourina, P. Plateau, S. Blanquet
- Biology, ChemistryThe Journal of Biological Chemistry
- 20 October 2000
The results indicate that an unexpected high number of d-amino acids can impair the bacterium growth through the accumulation ofd-Aminoacyl-tRNA molecules and that d-Tyr-tRNATyr deacylase has a specificity broad enough to recycle any of these molecules.
Critical role of the acceptor stem of tRNAs(Met) in their aminoacylation by Escherichia coli methionyl-tRNA synthetase.
- T. Meinnel, Y. Mechulam, C. Lazennec, S. Blanquet, G. Fayat
- Biology, ChemistryJournal of molecular biology
- 5 January 1993
It is proposed that, beyond the binding of the anticodon loop to the synthetase, the sequence of the acceptor stem may strongly influence the rate of the catalytic step of the aminoacylation reaction by properly orientating the 3'-end of the tRNA towards the catalysttic centre.