Isolation and Characterization of a Mitochondrially Synthesized Polypeptide from Neurospora crassa cni-1 Mutant

Michel, Rainer; Liebl, Anton; Machleidt, Werner; Otto, Joachim; Neupert, Walter

doi:10.1515/bchm2.1975.356.2.1595

Cited by 8 publications

(3 citation statements)

References 2 publications

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“…This could also be the reason why an intramitochondrially synthesized low-molecular-weight proteolipid was not found in the N. crussu ATPase complex [31]. On the other hand, an intramitochondrially synthesized polypeptide resembling the dicyclohexylcarbodiimide-binding proteolipid has been isolated from the nuclear mutant CNII of N. crussu and partially sequenced [37]. However, the function of this peptide, which is found only in traces in wild-type cells, is completely unknown.…”

Section: Discussionmentioning

confidence: 99%

Identification of an Intramitochondrially Synthesized Proteolipid Associated with the Mitochondrial ATPase Complex as the Product of a Mitochondrial Gene Determining Oligomycin Resistance in Aspergillus nidulans

et al. 1977

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An extranuclear oligomycin‐resistant mutant of Aspergillus nidulans was isolated and biochemically analyzed. The mutant grows slowly in the absence of oligomycin and contains an excess of cytochrome c. The ATPase complex solubilized from mutant mitochondria with Triton X‐100 is 80 times more resistant to oligomycin than the enzyme of the parental strain. The enzyme complexes of both strains were further purified to electrophoretic homogeneity and resolved by dodecylsulfate gel electrophoresis in the presence of 8 M urea into 16 polypeptide bands of apparent molecular weights between 65000 and 6000. Four proteins of apparent molecular weights 43000, 21000, 11000 and 6000 are synthesized on cycloheximide‐resistant mitochondrial ribosomes. The smallest subunit is selectively extracted from the purified enzyme by neutral chloroform/methanol (2/1). A proteolipid of identical electrophoretic mobility and site of synthesis is the major component of proteins extractable with the same solvent from whole mitochondrial membranes. This protein has been isolated from the mutant and its parental strain, and purified to apparent homogeneity. The proteins from both strains start with N‐formyl‐methionine and end with valine. However, a second internal methionine residue present in the wild‐type protein is absent, together with some other amino acids, from the mutant protein. It is concluded that this small lipophilic protein is coded by a mitochondrial gene determining oligomycin resistance, is synthesized on mitochondrial ribosomes and is associated with the membrane sector of the ATPase complex. The mutational alteration of the protein not only confers oligomycin resistance to the ATPase complex but also causes a structural alteration of the mitochondrial inner membrane.

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Section: Discussionmentioning

confidence: 99%

Identification of an Intramitochondrially Synthesized Proteolipid Associated with the Mitochondrial ATPase Complex as the Product of a Mitochondrial Gene Determining Oligomycin Resistance in Aspergillus nidulans

et al. 1977

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“…We were not able to isolate a five-subunit F 1 from Neurospora in the absence of the protease inhibitor phenylmethylsulfonylfluoride. It has been discussed that some chloroform/methanol-soluble proteins of low molecular weight originate from the proteolytic break-down of larger hydrophobic proteins [64].…”

Section: Saccharomycesmentioning

confidence: 99%

Biogenesis of mitochondrial ATPase

Sebald¹

1977

Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics

112

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“…When gels were stained with Coomassie Brillant Blue a protein distribution was found which coincided with the homogeneous 14 These findings suggest: a) that preparations of Neurospora mitochondria contain proteolytic enzyme activity and that this activity decreases with increasing periods of cycloheximide treatment of cells; b) that proteolysis takes place after dissolving the mitochondria with sodium dodecylsulfate; c) that mitochondrial translation products are more resistant to proteinase than cytoplasmic translation products, especially those with apparent molecular weights of about 20 000.…”

Section: Proteolytic Degradation Of Mitochondrial Proteinsmentioning

confidence: 63%

Action of Intracellular Proteinases on Mitochondrial Translation Products ofNeurospora crassaandSchizosaccharomyces pombe

Michel¹,

Liebl²,

Hartmann³

et al. 1976

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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Isolation and Characterization of a Mitochondrially Synthesized Polypeptide from Neurospora crassa cni-1 Mutant

Cited by 8 publications

References 2 publications

Identification of an Intramitochondrially Synthesized Proteolipid Associated with the Mitochondrial ATPase Complex as the Product of a Mitochondrial Gene Determining Oligomycin Resistance in Aspergillus nidulans

Identification of an Intramitochondrially Synthesized Proteolipid Associated with the Mitochondrial ATPase Complex as the Product of a Mitochondrial Gene Determining Oligomycin Resistance in Aspergillus nidulans

Biogenesis of mitochondrial ATPase

Action of Intracellular Proteinases on Mitochondrial Translation Products ofNeurospora crassaandSchizosaccharomyces pombe

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