Mitochondrial methionyl-tRNA(f)(Met) formyltransferase from Saccharomyces cerevisiae: Gene disruption and tRNA substrate specificity
| Autor: | Sylvain Blanquet, Yves Mechulam, Lionel Vial, Pilar Gomez, Michel Panvert, Emmanuelle Schmitt |
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| Přispěvatelé: | Physics of Living Systems, Laboratoire de Biochimie de l'Ecole polytechnique (BIOC), École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Mutant
MESH: Escherichia coli Proteins MESH: Amino Acid Sequence MESH: Base Sequence Mitochondrion medicine.disease_cause Biochemistry Saccharomyces Substrate Specificity MESH: Saccharomyces cerevisiae Proteins MESH: Genetic Vectors MESH: Esters Protein biosynthesis MESH: Animals MESH: Gene Silencing MESH: Oxygen Consumption Base Pairing biology Escherichia coli Proteins Esters Mitochondria MESH: Cattle Transfer RNA Hydroxymethyl and Formyl Transferases RNA Transfer Met Saccharomyces cerevisiae Proteins MESH: Mitochondria MESH: Hydroxymethyl and Formyl Transferases MESH: Base Pairing Genes Fungal Genetic Vectors Molecular Sequence Data Saccharomyces cerevisiae Catalysis Oxygen Consumption medicine Animals Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Gene Silencing Escherichia coli MESH: Humans MESH: Molecular Sequence Data Base Sequence MESH: RNA Transfer Met RNA MESH: Catalysis biology.organism_classification Mutagenesis Insertional MESH: Mutagenesis Insertional MESH: Substrate Specificity Cattle MESH: Genes Fungal |
| Zdroj: | Biochemistry, 42(4), 932-939. American Chemical Society Vial, L, Gomez, P, Panvert, M, Schmitt, E, Blanquet, S & Mechulam, Y 2003, ' Mitochondrial methionyl-tRNA(f)(Met) formyltransferase from Saccharomyces cerevisiae: Gene disruption and tRNA substrate specificity ', Biochemistry, vol. 42, no. 4, pp. 932-939 . https://doi.org/10.1021/bi026901x Biochemistry Biochemistry, American Chemical Society, 2003, 42 (4), pp.932-9. ⟨10.1021/bi026901x⟩ |
| ISSN: | 0006-2960 1520-4995 |
| DOI: | 10.1021/bi026901x |
| Popis: | International audience; Initiation of protein synthesis in bacteria, mitochondria, and chloroplasts involves a formylated methionyl-tRNA species. Formylation of this tRNA is catalyzed by a methionyl-tRNA(f)(Met) formyltransferase (formylase). Upon inactivation of the gene encoding formylase, the growth rate of Escherichia coli is severely decreased. This behavior underlines the importance of formylation to give tRNA(Met) an initiator identity. Surprisingly, however, recent data [Li, Y., Holmes, W. B., Appling, D. R., and RajBhandary, U. L. (2000) J. Bacteriol. 182, 2886-2892] showed that the respiratory growth of Saccharomyces cerevisiaewas not sensitive to deprivation of the mitochondrial formylase. In the present study, we report conditions of temperature or of growth medium composition in which inactivation of the formylase gene indeed impairs the growth of a S. cerevisiae haploid strain. Therefore, some selective advantage can eventually be associated to the existence of a formylating activity in the fungal mitochondrion under severe growth conditions. Finally, the specificity toward tRNA of S. cerevisiae mitochondrial formylase was studied using E. coli initiator tRNA and mutants derived from it. Like its bacterial counterpart, this formylase recognizes nucleotidic features in the acceptor stem of mitochondrial initiator tRNA. This behavior markedly distinguishes the mitochondrial formylase of yeast from that of animals. Indeed, it was shown that bovine mitochondrial formylase mainly recognizes the side chain of the esterified methionine plus a purine-pyrimidine base pair in the D-stem of tRNA [Takeuchi, N., Vial, L., Panvert, M., Schmitt, E., Watanabe, K., Mechulam, Y., and Blanquet, S. (2001) J. Biol. Chem. 276, 20064-20068]. Distinct tRNA recognition mechanisms adopted by the formylases of prokaryotic, fungal, or mammalian origins are likely to reflect coevolution of these enzymes with their tRNA substrate. Each mechanism appears well suited to an efficient selection of the substrate within the pool of all tRNAs. |
| Databáze: | OpenAIRE |
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