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Eukaryotic Cell, February 2005, p. 337-345, Vol. 4, No. 2
1535-9778/05/$08.00+0     doi:10.1128/EC.4.2.337-345.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Alteration of a Novel Dispensable Mitochondrial Ribosomal Small-Subunit Protein, Rsm28p, Allows Translation of Defective COX2 mRNAs

Elizabeth H. Williams,{dagger} Nada Bsat, Nathalie Bonnefoy,{ddagger} Christine A. Butler, and Thomas D. Fox*

Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York

Received 17 November 2004/ Accepted 6 December 2004

Mutations affecting the RNA sequence of the first 10 codons of the Saccharomyces cerevisiae mitochondrial gene COX2 strongly reduce translation of the mRNA, which encodes the precursor of cytochrome c oxidase subunit II. A dominant chromosomal mutation that suppresses these defects is an internal in-frame deletion of 67 codons from the gene YDR494w. Wild-type YDR494w encodes a 361-residue polypeptide with no similarity to proteins of known function. The epitope-tagged product of this gene, now named RSM28, is both peripherally associated with the inner surface of the inner mitochondrial membrane and soluble in the matrix. Epitope-tagged Rsm28p from Triton X-100-solubilized mitochondria sedimented with the small subunit of mitochondrial ribosomes in a sucrose gradient containing 500 mM NH4Cl. Complete deletion of RSM28 caused only a modest decrease in growth on nonfermentable carbon sources in otherwise wild-type strains and enhanced the respiratory defect of the suppressible cox2 mutations. The rsm28 null mutation also reduced translation of an ARG8m reporter sequence inserted at the COX1, COX2, and COX3 mitochondrial loci. We tested the ability of RSM28-1 to suppress a variety of cox2 and cox3 mutations and found that initiation codon mutations in both genes were suppressed. We conclude that Rsm28p is a dispensable small-subunit mitochondrial ribosomal protein previously undetected in systematic investigations of these ribosomes, with a positive role in translation of several mitochondrial mRNAs.

* Corresponding author. Mailing address: Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703. Phone: (607) 254-4835. Fax: (607) 255-6249. E-mail: tdf1{at}cornell.edu.

{dagger} Present address: Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Md.

{ddagger} Present address: Centre de Génétique Moléculaire, Laboratoire propre du CNRS associé à l'Université Pierre et Marie Curie, Gif-sur-Yvette, France.

Eukaryotic Cell, February 2005, p. 337-345, Vol. 4, No. 2
1535-9778/05/$08.00+0     doi:10.1128/EC.4.2.337-345.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jia, L., Kaur, J., Stuart, R. A. (2009). Mapping of the Saccharomyces cerevisiae Oxa1-Mitochondrial Ribosome Interface and Identification of MrpL40, a Ribosomal Protein in Close Proximity to Oxa1 and Critical for Oxidative Phosphorylation Complex Assembly. Eukaryot Cell 8: 1792-1802 [Abstract] [Full Text]  
  • Williams, E. H., Butler, C. A., Bonnefoy, N., Fox, T. D. (2007). Translation Initiation in Saccharomyces cerevisiae Mitochondria: Functional Interactions Among Mitochondrial Ribosomal Protein Rsm28p, Initiation Factor 2, Methionyl-tRNA-Formyltransferase and Novel Protein Rmd9p. Genetics 175: 1117-1126 [Abstract] [Full Text]  


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