Nucleic Acids Research, 2003, Vol. 31, No. 14 4218-4226
© 2003 Oxford University Press
Temperature-sensitive mutation in yeast mitochondrial ribosome recycling factor (RRF)
1 Department of Biochemistry and Molecular Pharmacology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, PA 19107-5541, USA, 2 Department of Biochemistry, Drexel University, College of Medicine, Philadelphia, PA 19102, USA, 3 Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA and 4 UMR Physiologie Moléculaire des Semences, F-49045 Angers, France
*To whom correspondence should be addressed at Department of Biochemistry and Molecular Pharmacology, Jefferson Medical College, Room 456A, 1020 Locust Street, Philadelphia, PA 19107-5541, USA. Tel: +1 215 503 6547; Fax: +1 215 923 7343; Email: hideko.kaji{at}mail.tju.edu
Present address:
Go Hirokawa, Department of Clinical Biochemistry, Graduate School of Pharmaceutical Sciences, Chiba University, Inage-ku, Chiba 263-8522, Japan
The yeast protein Rrf1p encoded by the FIL1 nuclear gene bears significant sequence similarity to Escherichia coli ribosome recycling factor (RRF). Here, we call FIL1 Ribosome Recycling Factor of yeast, RRF1. Its gene product, Rrf1p, was localized in mitochondria. Deletion of RRF1 leads to a respiratory incompetent phenotype and to instability of the mitochondrial genome (conversion to rho–/rho0 cytoplasmic petites). Yeast with intact mitochondria and with deleted genomic RRF1 that harbors a plasmid carrying RRF1 was prepared from spores of heterozygous diploid yeast. Such yeast with a mutated allele of RRF1, rrf1-L209P, grew on a non-fermentable carbon source at 30 but not at 36°C, where mitochondrial but not total protein synthesis was 90% inhibited. We propose that Rrf1p is essential for mitochondrial protein synthesis and acts as a RRF in mitochondria.
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