The membrane domain of complex I is not assembled in the stopper mutant E35 of Neurospora.
The assembly of mitochondrial NADH: ubiquinone oxidoreductase (complex I) was studied in the E35 stopper mutant of Neurospora crassa at different times during growth in liquid media. Assembly of complex I as well as of its membrane domain is impaired in this strain throughout the growth period. Nevertheless, a structure that resembles the peripheral aim of the enzyme is still formed in the mitochondria of this mutant. The absence of the membrane domain of complex I in E35 can be attributed to the specific deletion of the mitochondrial ND2 and ND3 subunits of the enzyme.
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Instituto de Ciências Biomédicas de Abel Salazar, Universidade do Porto, Portugal.
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D017353:Gene Deletion; D005800:Genes, Fungal; D007425:Intracellular Membranes / Q000201:enzymology*; D008928:Mitochondria / Q000201:enzymology* / Q000648:ultrastructure; D009154:Mutation; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000737:chemistry*; D009491:Neurospora / Q000235:genetics*; D010446:Peptide Fragments / Q000235:genetics; D017434:Protein Structure, Tertiary
D010446:Peptide Fragments; D016660:NAD(P)H Dehydrogenase (Quinone)