Characterisation of the last Fe-S cluster-binding subunit of Neurospora crassa complex I.
We have cloned cDNAs encoding the last iron-sulphur protein of complex I from Neurospora crassa. The cDNA sequence contains an open reading frame that codes for a precursor polypeptide of 226 amino acid residues with a molecular mass of 24972 Da. Our results indicate that the mature protein belongs probably to the peripheral arm of complex I and is rather unstable when not assembled into the enzyme. The protein is highly homologous to the PSST subunit of bovine complex I, the most likely candidate to bind iron-sulphur cluster N-2. All the amino acid residues proposed to bind such a cluster are conserved in the fungal protein.
Sousa
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Instituto de Ciências Biomédicas de Abel Salazar, Universidade do Porto, Porto, Portugal.
Barquera
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Duarte
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Finel
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Videira
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D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000096:biosynthesis / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000235:genetics*; D009492:Neurospora crassa / Q000235:genetics*; D016415:Sequence Alignment
D018076:DNA, Complementary; D007506:Iron-Sulfur Proteins; D016660:NAD(P)H Dehydrogenase (Quinone)