In Vitro Mutagenesis of the Mitochondrial Leucyl-tRNA Synthetase of S. Cerevisiae Reveals Residues Critical for Its in Vivo Activities

Overview

Journal Curr Genet

Specialty Genetics

Date 1992 Jul 1

PMID 1611670

Citations 5

Authors

G Y Li

C J Herbert

M Labouesse

P P SLONIMSKI

Affiliations

Soon will be listed here.

Abstract

The mitochondrial leucyl-tRNA synthetase (mLRS) of Saccharomyces cerevisiae is involved in both mitochondrial protein synthesis and pre-mRNA splicing. We have created mutations in the regions HIGH, GWD and KMSKS, which are involved in ATP-, amino acid- and tRNA-binding respectively, and which have been conserved in the evolution of group I tRNA synthetases. The mutants GRD and NMSKS have no discernible phenotype. The mutants AWD and ARD act as null alleles and lead to the production of 100% cytoplasmic petites. The mutants HIGN, NIGH and KMSNS are unable to grow on glycerol even in the presence of an intronless mitochondrial genome and accumulate petites to a greater extent than the wild-type but less than 40%. Experiments with an imported bI4 maturase indicate that the lesion in these mutations primarily affects the synthetase and not the splicing functions.

Citing Articles

The phenotypic expression of mitochondrial tRNA-mutations can be modulated by either mitochondrial leucyl-tRNA synthetase or the C-terminal domain thereof.

Giordano C, Morea V, Perli E, dAmati G Front Genet. 2015; 6:113.

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The isolated carboxy-terminal domain of human mitochondrial leucyl-tRNA synthetase rescues the pathological phenotype of mitochondrial tRNA mutations in human cells.

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Genetic evidence for interaction between Cbp1 and specific nucleotides in the 5' untranslated region of mitochondrial cytochrome b mRNA in Saccharomyces cerevisiae.

Chen W, Dieckmann C Mol Cell Biol. 1997; 17(11):6203-11.

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In vitro mutagenesis of the mitochondrial leucyl tRNA synthetase of Saccharomyces cerevisiae shows that the suppressor activity of the mutant proteins is related to the splicing function of the wild-type protein.

Li G, Becam A, SLONIMSKI P, Herbert C Mol Gen Genet. 1996; 252(6):667-75.

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