Partial suppression of the respiratory defect of qrs1/her2 glutamyl-tRNA amidotransferase mutants by overexpression of the mitochondrial pentatricopeptide Msc6p

Current Genetics
Bruno S ModaMario H Barros

Abstract

Recently, a large body of evidences indicates the existence in the mitochondrial matrix of foci that contain different proteins involved in mitochondrial RNA metabolism. Some of these proteins have a pentatricopeptide repeat motif that constitutes their RNA-binding structures. Here we report that MSC6, a mitochondrial pentatricopeptide protein of unknown function, is a multi copy suppressor of mutations in QRS1/HER2 a component of the trimeric complex that catalyzes the transamidation of glutamyl-tRNAQ to glutaminyl-tRNAQ. This is an essential step in mitochondrial translation because of the lack of a specific mitochondrial aminoacyl glutaminyl-tRNA synthetase. MSC6 over-expression did not abolish translation of an aberrant variant form of Cox2p detected in QRS1/HER2 mutants, arguing against a suppression mechanism that bypasses Qrs1p function. A slight decrement of the mitochondrial translation capacity as well as diminished growth on respiratory carbon sources media for respiratory activity was observed in the msc6 null mutant. Additionally, the msc6 null mutant did not display any impairment in RNA transcription, processing or turnover. We concluded that Msc6p is a mitochondrial matrix protein and further studies are require...Continue Reading

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Citations

Apr 14, 2017·Molecular Biology of the Cell·Mario H Barros, Alexander Tzagoloff
Nov 22, 2017·Cell Biology International·Raquel Fonseca Guedes-MonteiroMario H Barros
Aug 10, 2018·Molecular Biology of the Cell·Braulio Vargas Möller-HergtMartin Ott
Feb 16, 2019·The FEBS Journal·Leticia Veloso Ribeiro FrancoMario H Barros
Apr 17, 2018·Royal Society Open Science·William Irvin Sellers, Eishi Hirasaki

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