The primary structure of human Rieske iron-sulfur protein of mitochondrial cytochrome bc1 complex deduced from cDNA analysis.
We isolated a cDNA encoding human Rieske Fe-S protein of mitochondrial cytochrome bc1 complex from a fibroblast cDNA library by colony hybridization. The cDNA contains the nucleotide sequence encoding all of the amino acids (274 residues) comprising the putative precursor to the protein. Based on the known amino acid sequence of bovine Rieske Fe-S protein, the N-terminal extension sequence is presumed to be composed of 78 amino acids with a molecular weight of 8053. The mature protein consists of the same number of amino acid residues as that of its rat and bovine counterparts, having a homology of about 92% with the latter.
Nishikimi
M
M
Department of Biomedical Chemistry, Faculty of Medicine, University of Nagoya, Japan.
Hosokawa
Y
Y
Toda
H
H
Suzuki
H
H
Ozawa
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002417:Cattle; D004247:DNA / Q000235:genetics*; D014450:Electron Transport Complex III / Q000235:genetics*; D006801:Humans; D007506:Iron-Sulfur Proteins / Q000235:genetics; D008667:Metalloproteins / Q000235:genetics; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; C037989:Rieske iron-sulfur protein; D004247:DNA; D014450:Electron Transport Complex III