Nucleic Acids Research, 2001, Vol. 29, No. 17 3631-3637
© 2001 Oxford University Press
Rpm2p: separate domains promote tRNA and Rpm1r maturation in Saccharomyces cerevisiae mitochondria
Department of Biochemistry and Molecular Biology, School of Medicine, University of Louisville, Health Sciences Center, Louisville, KY 40292, USA
Rpm2p is a protein subunit of yeast mitochondrial RNase P and is also required for the maturation of Rpm1r, the mitochondrially-encoded RNA subunit of the enzyme. Previous work demonstrated that an insertional disruption of RPM2, which produces the C-terminally truncated protein Rpm2-
Cp, supports growth on glucose but cells lose some or all of their mitochondrial genome and become petite. These petites, even if they retain the RPM1 locus, lose their ability to process the 5'-ends of mitochondrial tRNA. We report here that if strains containing the truncated RPM2 allele are created and maintained on respiratory carbon sources they have wild-type mitochondrial genomes, and a significant portion of tRNA transcripts are processed. In contrast, precursor Rpm1r transcripts accumulate and mature Rpm1r is not made. These data show that one function of the deleted C-terminal region is in the maturation of Rpm1r, and that this region and mature Rpm1r are not absolutely required for RNase P activity. Finally, we demonstrate that full activity can be restored if the N-terminal and C-terminal domains of Rpm2p are supplied in trans.
* To whom correspondence should be addressed. Tel: +1 502 852 7797; Fax: +1 502 852 6222; Email: ncmart01{at}gwise.louisville.edu Present addresses:Guo-Jian Gao, BD PharMingen, 10975 Torreyana Road, San Diego, CA 92121-1106, USAPavol Sulo, Department of Biochemistry, Comenius University, Mlynska Dolina CH1-227, 84215 Bratislava, Slovakia The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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