A nuclear mutation that post-transcriptionally blocks accumulation of a yeast mitochondrial gene product can be suppressed by a mitochondrial gene rearrangement

Müller, Peter; Reif, Michelle K.; Shen, Zhemin; Sengstag, Christian; Mason, Thomas L.; Fox, Thomas D.

doi:10.1016/0022-2836(84)90178-5

Cited by 112 publications

(48 citation statements)

References 38 publications

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“…(McMullin et al, 1990;Haffter et al, 1991;Haffter and Fox, 1992) and interactions between of Nam1p and Rpo41p (mitochondrial RNA polymerase) (Rodeheffer et al, 2001) were reported previously. Two-hybrid and genetic interactions among Pet54p, Pet122p, and Pet494p were reported previously (Brown et al, 1994;Wiesenberger et al, 1995). without eliminating respiratory complex formation, by in vivo expression of chimeric mRNAs containing 5Ј-UTLs and coding sequences derived from different respiratory complex genes (Mü ller et al, 1984;Fox, 1986, 1988;Poutre and Fox, 1987;Rö del and Fox, 1987;Mulero and Fox, 1993b;Manthey and McEwen, 1995). Thus, although the interactions among translational activators for the core cytochrome c oxidase subunits are likely to confer a selective advantage, they are not absolutely required to form the enzyme.…”

Section: Discussionmentioning

confidence: 95%

Interactions amongCOX1,COX2, andCOX3mRNA-specific Translational Activator Proteins on the Inner Surface of the Mitochondrial Inner Membrane ofSaccharomyces cerevisiae

Naithani

Saracco

Butler

et al. 2003

MBoC

Self Cite

144

117

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The core of the cytochrome c oxidase complex is composed of its three largest subunits, Cox1p, Cox2p, and Cox3p, which are encoded in mitochondrial DNA of Saccharomyces cerevisiae and inserted into the inner membrane from the inside. Mitochondrial translation of the COX1,COX2, and COX3 mRNAs is activated mRNA specifically by the nuclearly coded proteins Pet309p, Pet111p, and the concerted action of Pet54p, Pet122p, and Pet494p, respectively. Because the translational activators recognize sites in the 5′-untranslated leaders of these mRNAs and because untranslated mRNA sequences contain information for targeting their protein products, the activators are likely to play a role in localizing translation. Herein, we report physical associations among the mRNA-specific translational activator proteins, located on the matrix side of the inner membrane. These interactions, detected by coimmune precipitation and by two-hybrid experiments, suggest that the translational activator proteins could be organized on the surface of the inner membrane such that synthesis of Cox1p, Cox2p, and Cox3p would be colocalized in a way that facilitates assembly of the core of the cytochrome c oxidase complex. In addition, we found interactions between Nam1p/Mtf2p and the translational activators, suggesting an organized delivery of mitochondrial mRNAs to the translation system.

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Section: Discussionmentioning

confidence: 95%

Interactions amongCOX1,COX2, andCOX3mRNA-specific Translational Activator Proteins on the Inner Surface of the Mitochondrial Inner Membrane ofSaccharomyces cerevisiae

Naithani

Saracco

Butler

et al. 2003

MBoC

Self Cite

144

117

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“…S. cerevisiae DAl (MATa ade2) and a [rhoo] derivative of DAl (35) were obtained from Tom Fox. Yeast cells were grown at 30°C in YPEG medium containing 1% (wt/vol) yeast extract, 2% (wt/vol) peptone, 3% (vol/vol) ethanol, and 3% (vol/vol) glycerol.…”

Section: Methodsmentioning

confidence: 99%

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene.

McMullin¹,

Hallberg²

1988

Mol. Cell. Biol.

225

122

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We recently reported that a Tetrahymena thermophila 58-kilodaltodi (kDa) mitochondrial protein (hsp58) was selectively synthesized during heat shock. In this study, we show that hsp58 displayed antigenic similarity with mitochondrially associated proteins from Saccharomyces cerevisiae (64 kDa), Xenopus laevis (60 kDa), Zea mays (62 kDa), and human cells (59 kDa). Furthermore, a 58-kDa protein from Eschenchia coli also exhibited antigenic cross-reactivity to an antiserum directed against the T. thermophila mitochondrial protein. The proteins from S. cerevisiae and E. coli antigenically related to hsp58 were studied in detail and found to share several other characteristics with hsp58, including heat inducibility and the property of associating into distinct oligomeric complexes. The T. thermophila, S. cerevisiae, and E. coli macromolecular complexes containing these related proteins had similar sedimentation characteristics and virtually identical morphologies as seen with the electron microscope. The distinctive properties of the E. coli homolog to T. thermophila hsp58 indicate that it is most likely the product of the groEL gene.Most organisms subjected to sublethal heat shock-inducing temperatures become conditioned to survive at even higher, normally lethal, temperatures. The acquisition of this thermotolerant state is accompanied by the production of specific arrays of polypeptides, collectively known as heat shock proteins (HSPs), which are thought to be involved in protecting the organism from hyperthermic stress (for reviews, see references 8 and 32). Several of these proteins have been shown to exhibit a relatively high degree of evolutionary conservation in their DNA and amino acid sequences (2-5, 12, 24-26, 28), as well as in their subcellular compartmentalization (1,30,45,47). This conservation of structure and localization within the cell strongly suggests that these proteins perform similar functions in the different species in which these proteins are found.In Tetrahymena thermophila, shifting cells to 37 through 41°C induces the selective synthesis of a specific array of HSPs (16,18,19,33,49). Recently, we purified and characterized a minor member of this set of proteins. We find that not only is this protein, hsp58, one of the proteins selectively synthesized and accumulated early in heat shock, but it is also a normal component of the mitochondria of this organism. Heat shock causes the level of hsp58 to increase approximately two-to threefold, and this protein also accumulates specifically in mitochondria. Another interesting property of hsp58 is that it assembles into large oligomeric complexes consisting primarily of the hsp58 protein (34).Since at least two of the HSPs of T. thermophila, hsp73 and hsp80, exhibit evolutionary conservation with HSPs of other species (18), we decided to ask whether homologs of hsp58 also exist in other organisms. This was done by using an antiserum prepared against highly purified hsp58 (34) to probe protein samples from several diverse species. In this study, ...

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“…The rapid loss of respiratory function, even under selective conditions, suggested that the revertants might be heteroplasmic cells containing both the wildtype and suppressor r À genomes. This type of mitochondrial suppressor has been reported for a number of mitochondrial protein-coding genes that fail to be expressed because of mutations in nuclear gene products that promote translation of the mRNAs by interacting with their 59-UTRs (Dieckmann et al 1984;Muller et al 1984;Rodel and Fox 1987;Manthey and McEwen 1995). The presence in W303DATP22/ R3 of a suppressor r À genome was confirmed by the mitochondrial genotypes of 104 respiratory-deficient segregants (Table 3).…”

Section: Resultsmentioning

confidence: 58%

“…Mitochondrial r À genomes with heterologous 59 upstream sequences have been shown to suppress mutations in translation factors for COX1 (Manthey and McEwen 1995), COX2 (Poutre and Fox 1987), COX3 (Muller et al 1984), and COB (Rodel and Fox 1987). These transcript-specific translation factors interact with the 59-UTRs of their cognate mRNAs.…”

Section: Discussionmentioning

confidence: 99%

The Saccharomyces cerevisiae ATP22 Gene Codes for the Mitochondrial ATPase Subunit 6-Specific Translation Factor

2007

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Mutations in the Saccharomyces cerevisiae ATP22 gene were previously shown to block assembly of the F 0 component of the mitochondrial proton-translocating ATPase. Further inquiries into the function of Atp22p have revealed that it is essential for translation of subunit 6 of the mitochondrial ATPase. The mutant phenotype can be partially rescued by the presence in the same cell of wild-type mitochondrial DNA and a r À deletion genome in which the 59-UTR, first exon, and first intron of COX1 are fused to the fourth codon of ATP6. The COX1/ATP6 gene is transcribed and processed to the mature mRNA by splicing of the COX1 intron from the precursor. The hybrid protein translated from the novel mRNA is proteolytically cleaved at the normal site between residues 10 and 11 of the subunit 6 precursor, causing the release of the polypeptide encoded by the COX1 exon. The ability of the r À suppressor genome to express subunit 6 in an atp22 null mutant constitutes strong evidence that translation of subunit 6 depends on the interaction of Atp22p with the 59-UTR of the ATP6 mRNA.

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A nuclear mutation that post-transcriptionally blocks accumulation of a yeast mitochondrial gene product can be suppressed by a mitochondrial gene rearrangement

Cited by 112 publications

References 38 publications

Interactions amongCOX1,COX2, andCOX3mRNA-specific Translational Activator Proteins on the Inner Surface of the Mitochondrial Inner Membrane ofSaccharomyces cerevisiae

Interactions amongCOX1,COX2, andCOX3mRNA-specific Translational Activator Proteins on the Inner Surface of the Mitochondrial Inner Membrane ofSaccharomyces cerevisiae

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene.

The Saccharomyces cerevisiae ATP22 Gene Codes for the Mitochondrial ATPase Subunit 6-Specific Translation Factor

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