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Nucleic Acids Research, 1990, Vol. 18, No. 6 1521-1529
© 1990

MOLECULAR BIOLOGY

Cloning and characterization of nuclear genes for two mitochondrial ribosomal proteins in Saccharomyces cerevisiae

Madoka Kitakawa*, Lutz Grohmann1, Hanns-Rüdiger Graack and Katsumi Isono

Department of Biology, Faculty of Science, Kobe University Rokkodai, Nada-ku, Kobe 657, Japan 1Max-Planck-Institut für Molekulare Genetik Abteilung Wittmann, Ihnestrasse 73, D-1000 Berlin 33, FRG

*To whom Correspondence should be addressed

Received November 28, 1989. Revised January 29, 1990. Accepted January 29, 1990.

The genes for two large subunit proteins, YmL8 and YmL20, of the mitochondrial ribosome of Saccharomyces cerevisiae were cloned by hybridization with synthetic oligonucleotide mixtures corresponding to their N-terminal amino acid sequences. They were termed MRP-L8 and MRP-L20, respectively, and their nucleotide sequences were determined using a DNA sequencer. The MRP-L8 gene was found to encode a 26.8-kDa protein whose deduced amino acid sequence has a high degree of similarity to ribosomal protein L17 of Escherichia coli. The gene MRP-L20 was found to encode a 22.3-kDa protein with a presequence consisting of 18 amino acid residues. By Southern blot hybridization to the yeast chromosomes separated by field-inversion gel electrophoresis, the MRP-L8 and MRP-L20 genes were located on chromosomes X and XI, respectively. Gene disruption experiments indicate that their products, YmL8 and YmL20 proteins, are essential for the mitochondrial function and the absence of these proteins causes instability of the mitochondrial DNA.


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