The most conserved nuclear-encoded polypeptide of cytochrome c oxidase is the putative zinc-binding subunit: primary structure of subunit V from the slime mold Dictyostelium discoideum.
A full-length 515 base pairs cDNA for cytochrome c oxidase subunit V of D. discoideum was isolated from a lambda gt11 expression library. The encoded polypeptide, whose identity was confirmed by partial protein sequencing, is 119 amino acids long (Mr = 13,352) and does not contain a cleavable presequence. The protein, which is homologous to human subunit Vb and yeast subunit IV, exhibits the highest degree of sequence conservation found among nuclear-encoded subunits of cytochrome c oxidase from distantly related organisms. All the invariant residues are clustered in two regions of the C-terminus which include the putative amino acids involved in the coordination of the Zn ion tightly associated to eukaryotic oxidase.
Rizzuto
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R
CNR Centro Studi per la Fisiologia dei Mitocondri, Università di Padova, Italy.
Sandonà
D
D
Brini
M
M
Capaldi
R A
RA
Bisson
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D005075:Biological Evolution; D004023:Dictyostelium / Q000201:enzymology* / Q000235:genetics; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D015032:Zinc / Q000378:metabolism
D003576:Electron Transport Complex IV; D015032:Zinc