M. Duarte et al., PRIMARY STRUCTURE OF A FERREDOXIN-LIKE IRON-SULFUR SUBUNIT OF COMPLEX-I FROM NEUROSPORA-CRASSA, Biochimica et biophysica acta. Bioenergetics, 1275(3), 1996, pp. 151-153
We have isolated cDNA clones encoding an iron-sulfur polypeptide subun
it of the mitochondrial complex I of Neurospora crassa. The fungal cDN
A library was screened by hybridisation with an heterologous probe fro
m Paracoccus denitrificans. The DNA sequence of relevant isolates was
determined and revealed an open reading frame encoding a precursor pro
tein 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 f
rom bovine and P. denitrificans. Interestingly, an alanine residue wit
hin 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.