Biogenesis of mitochondria. Oli2 mutations affecting the coupling of oxidation to phosphorylation in Saccharomyces cerevisiae

Murphy, Mark; Roberts, Henry; Choo, Wan Mee; Macreadie, Ian; Marzuki, Sangkot; Lukins, H. B.; Linnane, Anthony W.

doi:10.1016/0005-2728(80)90090-0

Cited by 19 publications

(6 citation statements)

References 35 publications

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“…There were more electron transport genes upregulated than downregulated. In addition, subunit 6 of the mitochondrial ATPase, an enzyme complex that catalyzes coupling of proton flux (oxidative phosphorylation) to ATP synthesis (52), had elevated expression in atrophying RBT muscle. Furthermore, expression of several isoforms of creatine kinases was consistently upregulated in atrophying muscle.…”

Section: Genes Involved In Glucose Metabolismmentioning

confidence: 99%

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Salem

Kenney

Rexroad

et al. 2006

Physiological Genomics

115

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Salem M, Kenney PB, Rexroad CE 3rd, Yao J. Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model. Physiol Genomics 28: 33-45, 2006. First published August 1, 2006; doi:10.1152/physiolgenomics.00114.2006.-Muscle atrophy is a physiological response to diverse physiological and pathological conditions that trigger muscle deterioration through specific cellular mechanisms. Despite different signals, the biochemical changes in atrophying muscle share many common cascades. Muscle deterioration as a physiological response to the energetic demands of fish vitellogenesis represents a unique model for studying the mechanisms of muscle degradation in non-mammalian animals. A salmonid microarray, containing 16,006 cDNAs, was used to study the transcriptome response to atrophy of fast-switch muscles from gravid rainbow trout compared with sterile fish. Eighty-two unique transcripts were upregulated and 120 transcripts were downregulated in atrophying muscles. Transcripts having gene ontology identifiers were grouped according to their functions. Muscle deterioration was associated with elevated expression of genes involved in the catheptic and collagenase proteolytic pathways; the aerobic production, buffering, and utilization of ATP; and growth arrest; whereas atrophying muscle showed downregulation of genes encoding a serine proteinase inhibitor, enzymes of anaerobic respiration, muscle proteins as well as genes required for RNA and protein biosynthesis/processing. Therefore, gene transcription of the trout muscle atrophy changed in a manner similar to mammalian muscle atrophy. These changes result in an arrest of normal cell growth, protein degradation, and decreased glycolytic cellular respiration that is characteristic of the fast-switch muscle. For the first time, other changes/mechanisms unique to fish were discussed including genes associated with muscle atrophy. atrophy; Oncorhynchus mykiss SEVERAL PHYSIOLOGICAL and pathological conditions can cause muscle atrophy by triggering unique responses through distinct cellular stimuli. Transcriptional mechanisms of muscle wastage are well characterized at the transcriptome level in mammalian models as a response to nutritional restriction (7), fasting, severe diseases, including cancer, renal failure, diabetes (41, 42), and sepsis (42), as well as muscle disuse or denervation (4, 57). Some studies have dealt with fish muscle atrophy at the level of individual genes/mechanisms (46, 51, 58, 60 -62). The molecular basis of mammalian muscle atrophy has received considerable attention in the literature (25,30). Losing muscle mass results from elevated rate of proteolysis and decreased rate of protein synthesis. Despite the significant amount of literature (30,32,42), the specific roles of the proteolytic systems in degrading mammalian muscle still are unclear. Moreover, we recently showed that fish use different muscle degrading proteolytic strategies compared with mammals (58). The ubiquitin-proteasome pathway,...

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Section: Genes Involved In Glucose Metabolismmentioning

confidence: 99%

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Salem

Kenney

Rexroad

et al. 2006

Physiological Genomics

115

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“…A second subunit implicated in oxidative phosphorylation (Murphy et al, 1980) is also translated on mitochondrial ribosomes. This protein of mol.…”

Section: Introductionmentioning

confidence: 99%

Amino acid sequence of a new mitochondrially synthesized proteolipid of the ATP synthase of Saccharomyces cerevisiae.

Velours¹,

Esparza²,

Hoppe³

et al. 1984

The EMBO Journal

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The purification and the amino acid sequence of a proteolipid translated on ribosomes in yeast mitochondria is reported. This protein, which is a subunit of the A TP synthase, was purified by extraction with chloroform/methanol (2/1) and subsequent chromatography on phosphocellulose and reverse phase h.p.l.c. A mol. wt. of 5500 was estimated by chromatography on Bio-Gel P-30 in 8011/o fonnie acid. The complete amino acid sequence of this protein was determined by automated solid phase Edman degradation of the whole protein and of fragments obtained after cleavage with cyanogen bromide. The sequence analysis indicates a length of 48 amino acid residues. The calculated mol. wt. of 5870 corresponds to the value found by gel chromatography. This polypeptide contains three basic residues and no negatively charged side chain. The three basic residues are clustered at the C terminus. The primary structure of this protein is in full agreement with the predicted amino acid sequence of the putative polypeptide encoded by the mitochondrial aap1 gene recently discovered in Saccharomyces cerevisiae. Moreover, this protein shows 5011/o homology with the amino acid sequence of a putative polypeptide encoded by an unidentified reading frame also discovered near the mitochondrial ATPase subunit 6 genein Aspergillus nidulans.

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“…The otl gene codes for subunit 9, a 7.6 kilodalton (kd) proteolipid, as shown by a comparison of the amino acid sequence of the proteolipid (8) with that predicted by the nucleotide sequence of the oZil gene (9,10). The oti2 gene specifies mtATPase subunit 6, a polypeptide which has an apparent molecular weight of 20 kd based on its gel mobility and which is involved in the coupling of respiration and oxidative phosphorylation (11). This gene-protein relationship was deduced from analysis of a number of oU2 mitL mutants (unable to grow on non-fermentable substrates) in which the 20 kd polypeptide is replaced by smaller polypeptides that can be immunoprecipitated with anti-holo-mtATPase antibody (12,13).…”

Section: Introductionmentioning

confidence: 99%

Biogenesis of mitochondria: the mitochondrial gene (aap1) coding for mitochondrial ATPase subunit 8 inSaccharomyces cerevisiae

et al. 1983

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A mitochondrial gene (denoted aap1) in Saccharomyces cerevisiae has been characterized by nucleotide sequence analysis of a region of mtDNA between the oxi3 and oli2 genes. The reading frame of the aap1 gene specifies a hydrophobic polypeptide containing 48 amino acids. The functional nature of this reading frame was established by sequence analysis of a series of mit- mutants and revertants. Evidence is presented that the aap1 gene codes for a mitochondrially synthesized polypeptide associated with the mitochondrial ATPase complex. This polypeptide (denoted subunit 8) is a proteolipid whose size has been previously assumed to be 10 kilodaltons based on its mobility on SDS-polyacrylamide gels, but the sequence of the aap1 gene predicts a molecular weight of 5,815 for this protein.

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Biogenesis of mitochondria. Oli2 mutations affecting the coupling of oxidation to phosphorylation in Saccharomyces cerevisiae

Cited by 19 publications

References 35 publications

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Amino acid sequence of a new mitochondrially synthesized proteolipid of the ATP synthase of Saccharomyces cerevisiae.

Biogenesis of mitochondria: the mitochondrial gene (aap1) coding for mitochondrial ATPase subunit 8 inSaccharomyces cerevisiae

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