RPM2, independently of its mitochondrial RNase P function, suppresses an ISP42 mutant defective in mitochondrial import and is essential for normal growth.

Molecular and Cellular Biology
C K KassenbrockN C Martin

Abstract

RPM2 is identified here as a high-copy suppressor of isp42-3, a temperature-sensitive mutant allele of the mitochondrial protein import channel component, Isp42p. RPM2 already has an established role as a protein component of yeast mitochondrial RNase P, a ribonucleoprotein enzyme required for the 5' processing of mitochondrial precursor tRNAs. A relationship between mitochondrial tRNA processing and protein import is not readily apparent, and, indeed, the two functions can be separated. Truncation mutants lacking detectable RNase P activity still suppress the isp42-3 growth defect. Moreover, RPM2 is required for normal fermentative yeast growth, even though mitochondrial RNase P activity is not. The portion of RPM2 required for normal growth and suppression of isp42-3 is the same. We conclude that RPM2 is a multifunctional gene. We find Rpm2p to be a soluble protein of the mitochondrial matrix and discuss models to explain its suppression of isp42-3.

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Citations

Apr 6, 2006·Critical Reviews in Biochemistry and Molecular Biology·Scott C Walker, David R Engelke
Dec 6, 2011·Biochimica Et Biophysica Acta·Walter Rossmanith
Jun 5, 2002·Annual Review of Biochemistry·Shaohua XiaoDavid R Engelke
Jan 1, 1997·Annual Review of Biochemistry·W Neupert
Mar 10, 2001·Journal of Cellular Physiology·S XiaoD R Engelke
Nov 5, 2013·RNA Biology·Christopher J HerbertNathalie Bonnefoy
Jul 19, 2005·Molecular and Cellular Biology·Vilius StribinskisNancy C Martin
Jun 6, 2000·Microbiology and Molecular Biology Reviews : MMBR·V Contamine, M Picard
Jun 17, 1999·FEMS Microbiology Reviews·A Schön
Feb 13, 2003·Journal of Molecular Biology·Peter RehlingChristof Meisinger

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