Advanced search
Start date
Betweenand
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

Full text
Author(s):
Moda, Bruno S. [1] ; Ferreira-Junior, Jose Ribamar [2] ; Barros, Mario H. [1]
Total Authors: 3
Affiliation:
[1] Univ Sao Paulo, Dept Microbiol, Inst Ciencias Biomed, Ave Prof Lineu Prestes 1374, BR-05508900 Sao Paulo - Brazil
[2] Escola Artes Ciencias & Humanidades USP, Ave Arlindo Bettio 1000, BR-03828000 Sao Paulo - Brazil
Total Affiliations: 2
Document type: Journal article
Source: CURRENT GENETICS; v. 62, n. 3, p. 607-617, AUG 2016.
Web of Science Citations: 6
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 required to indicate the specific function of Msc6p in mitochondrial translation. (AU)

FAPESP's process: 13/09482-8 - Saccharomyces cerevisiae as a model for mitochondrial translation studies
Grantee:Mario Henrique de Barros
Support Opportunities: Regular Research Grants