RPM2, INDEPENDENTLY OF ITS MITOCHONDRIAL RNASE-P FUNCTION, SUPPRESSESAN ISP42 MUTANT DEFECTIVE IN MITOCHONDRIAL IMPORT AND IS ESSENTIAL FOR NORMAL GROWTH
Ck. Kassenbrock et al., RPM2, INDEPENDENTLY OF ITS MITOCHONDRIAL RNASE-P FUNCTION, SUPPRESSESAN ISP42 MUTANT DEFECTIVE IN MITOCHONDRIAL IMPORT AND IS ESSENTIAL FOR NORMAL GROWTH, Molecular and cellular biology, 15(9), 1995, pp. 4763-4770
RPM2 is identified here as a high-copy suppressor of isp42-3, a temper
ature-sensitive mutant allele of the mitochondrial protein import chan
nel component, Isp42p, RPM2 already has an established role as a prote
in component of yeast mitochondrial RNase P, a ribonucleoprotein enzym
e required for the 5' processing of mitochondrial precursor tRNAs, A r
elationship between mitochondrial tRNA processing and protein import i
s not readily apparent, and, indeed, the two functions can be separate
d, Truncation mutants lacking detectable RNase P activity still suppre
ss the isp42-3 growth defect, Moreover, RPM2 is required for normal fe
rmentative yeast growth, even though mitochondrial RNase P activity is
not, The portion of RPM2 required for normal growth and suppression o
f 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 an
d discuss models to explain its suppression of isp42-3.