Primary structure of a ferredoxin-like iron-sulfur subunit of complex I from Neurospora crassa.
We have isolated cDNA clones encoding an iron-sulfur polypeptide subunit of the mitochondrial complex I of Neurospora crassa. The fungal cDNA library was screened by hybridisation with an heterologous probe from Paracoccus denitrificans. The DNA sequence of relevant isolates was determined and revealed an open reading frame encoding a precursor protein of 219 amino acid residues. The gene product is a ferredoxin-like protein that contains two cysteine-rich motives that may each bind a tetranuclear iron-sulfur cluster. The primary structure of the protein is highly homologous to the 23 kDa iron-sulfur subunit of complex I from bovine and P. denitrificans. Interestingly, an alanine residue within the second cluster-binding motif, which is conserved in complex I but replaced by tyrosine in similar chloroplast genes, is substituted for serine in N. crassa.
Duarte
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Instituto de Ciências Biomédicas de Abel Salazar, Porto, Portugal.
Finel
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Videira
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D000595:Amino Acid Sequence; D001483:Base Sequence; D016384:Consensus Sequence; D018076:DNA, Complementary / Q000235:genetics; D042967:Electron Transport Complex I; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics*; D005800:Genes, Fungal; D007506:Iron-Sulfur Proteins / Q000235:genetics*; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics*; D009492:Neurospora crassa / Q000737:chemistry / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D005656:Fungal Proteins; D007506:Iron-Sulfur Proteins; D009247:NADH, NADPH Oxidoreductases; D042967:Electron Transport Complex I