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- W2089907350 abstract "The formation of cytochrome oxidase was examined in the cytochrome-aa3-deficient mi-3 cyto-plasmic mutant ofNeurospora crassa. The treatment of mitochondria of mutant mi-3 with antibody to cytochrome oxidase yields a precipitate of cross-reacting material consisting predominantly of cytochrome oxidase subunits 5 (mol. wt 14000) and 6 (mol. wt 12000) and small amounts of subunits 4 (mol. wt 16000) and 7 (mol. wt 10000), but devoid of the mitochondrially synthesized, high molecular weight polypeptides, namely subunits 1 (mol. wt 41000), 2 (mol. wt 28000) and 3 (mol. wt 21000). On the other hand, a qualitative examination of the products of mitochondrial translation in mutant mi-3 revealed that large molecular weight polypeptides are synthesized. However, a comparison of the dodecyl sulfate acrylamide gel electrophoresis patterns of the mitochondrial translation products of mutant mi-3 and wild-type indicated that the cytoplasmic mutant is deficient in polypeptides in the molecular weight ranges of 28000 and 21000, respectively. By means of subunit specific antibodies it could be shown that the mitochondria of mutant mi-3 contain virtually undetectable amounts of subunit 2 of cytochrome oxidase, but synthesize easily detectable quantities of subunits 1 and 3. Those subunits that are present in the mitochondria of mutant mi-3 do not appear to form a definitive complex with each other. The above results are discussed in view of earlier observations indicating that mutant mi-3 may be defective in a regulatory circuit that controls the formation of cytochrome aa3. The synthesis of subunit 2 of cytochrome oxidase could be the affected process, and the relative deficiency of this polypeptide may limit the assembly of cytochrome aa3 in the mutant." @default.
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- W2089907350 date "1977-10-01" @default.
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- W2089907350 title "Deficiency of Subunit Two of Cytochrome Oxidase in the mi-3 Cytoplasmic Mutant of Neurospora crassa" @default.
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- W2089907350 doi "https://doi.org/10.1111/j.1432-1033.1977.tb11844.x" @default.
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