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Nucleic Acids Research, 1993, Vol. 21, No. 23 5308-5315
© 1993

MOLECULAR BIOLOGY

Single point mutations in domain II of the yeast mitochondrial release factor mRF-1 affect ribosome binding

Herman J. Pel+, Martijn Rep, Hendrikus Jan Dubbink and Leslie A. Grivell*

Section for Molecular Biology, Department of Molecular Cell Biology, University of Amsterdam Kruislaan 318, 1098 SM Amsterdam, The Netherlands

*To whom correspondence should be addressed

Received September 27, 1993. Revised October 8, 1993. Accepted October 8, 1993.

We have recently described two yeast strains that are mutated in the MRF1 gene encoding the mitochondrial release factor mRF-1. Both mutants provoke genespecific defects in mitochondrial translational termination. In the present study we report the cloning, sequencing, as well as an analysis of residual activities of both mutant mrf1 alleles. Each allele specifies a different single amino acid substitution located one amino acid apart. The amino acid changes do not affect the level or cellular localization of the mutant proteins, since equal amounts of wild type and mutant mRF-1 were detected in the mitochondrial compartment. Overexpression of the mutant alleles in wild type and mrf1 mutant yeast strains produces a phenotype consistent with a reduced affinity of the mutant release factors for the ribosome, indicating that the mutations map in a release factor domain involved in ribosome binding. We also demonstrate that nonsense suppression caused by a mutation in the mitochondrial homolog of the E.coli small ribosomal protein S4 can be reversed by a slight over-expression of the MRF1 gene.

+Present address: Laboratoire de Geneuque Moleculaire, Institut de Gendtique et Microbiologie, University Paris-Sud, 91405 Orsay, France


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