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Research Article

NAM9 nuclear suppressor of mitochondrial ochre mutations in Saccharomyces cerevisiae codes for a protein homologous to S4 ribosomal proteins from chloroplasts, bacteria, and eucaryotes.

M Boguta, A Dmochowska, P Borsuk, K Wrobel, A Gargouri, J Lazowska, P P Slonimski, B Szczesniak, A Kruszewska
M Boguta
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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A Dmochowska
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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P Borsuk
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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K Wrobel
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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A Gargouri
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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J Lazowska
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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P P Slonimski
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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B Szczesniak
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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A Kruszewska
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
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DOI: 10.1128/MCB.12.1.402
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ABSTRACT

We report the genetic characterization, molecular cloning, and sequencing of a novel nuclear suppressor, the NAM9 gene from Saccharomyces cerevisiae, which acts on mutations of mitochondrial DNA. The strain NAM9-1 was isolated as a respiration-competent revertant of a mitochondrial mit mutant which carries the V25 ochre mutation in the oxi1 gene. Genetic characterization of the NAM9-1 mutation has shown that it is a nuclear dominant omnipotent suppressor alleviating several mutations in all four mitochondrial genes tested and has suggested its informational, and probably ribosomal, character. The NAM9 gene was cloned by transformation of the recipient oxi1-V25 mutant to respiration competence by using a gene bank from the NAM9-1 rho o strain. Orthogonal-field alternation gel electrophoresis analysis and genetic mapping localized the NAM9 gene on the right arm of chromosome XIV. Sequence analysis of the NAM9 gene showed that it encodes a basic protein of 485 amino acids with a presequence that could target the protein to the mitochondrial matrix. The N-terminal sequence of 200 amino acids of the deduced NAM9 product strongly resembles the S4 ribosomal proteins from chloroplasts and bacteria. Significant although less extensive similarity was found with ribosomal cytoplasmic proteins from lower eucaryotes, including S. cerevisiae. Chromosomal inactivation of the NAM9+ gene is not lethal to the cell but leads to respiration deficiency and loss of mitochondrial DNA integrity. We conclude that the NAM9 gene product is a mitochondrial ribosomal counterpart of S4 ribosomal proteins found in other systems and that the suppressor acts through decreasing the fidelity of translation.

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NAM9 nuclear suppressor of mitochondrial ochre mutations in Saccharomyces cerevisiae codes for a protein homologous to S4 ribosomal proteins from chloroplasts, bacteria, and eucaryotes.
M Boguta, A Dmochowska, P Borsuk, K Wrobel, A Gargouri, J Lazowska, P P Slonimski, B Szczesniak, A Kruszewska
Molecular and Cellular Biology Jan 1992, 12 (1) 402-412; DOI: 10.1128/MCB.12.1.402

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NAM9 nuclear suppressor of mitochondrial ochre mutations in Saccharomyces cerevisiae codes for a protein homologous to S4 ribosomal proteins from chloroplasts, bacteria, and eucaryotes.
M Boguta, A Dmochowska, P Borsuk, K Wrobel, A Gargouri, J Lazowska, P P Slonimski, B Szczesniak, A Kruszewska
Molecular and Cellular Biology Jan 1992, 12 (1) 402-412; DOI: 10.1128/MCB.12.1.402
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