Note. The novel nucleotide sequence data published here have been submitted to the EMBL sequence data bank and are available under accession number X 61590.
Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 203, Issue 3, pages 587–592, February 1992
How to Cite
DE VRIES, S., VAN WITZENBURG, R., GRIVELL, L. A. and MARRES, C. A. M. (1992), Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. European Journal of Biochemistry, 203: 587–592. doi: 10.1111/j.1432-1033.1992.tb16587.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received July 5/September 20, 1991) – EJB 91 0875
The gene encoding the yeast mitochondrial rotenone-insensitive internal NADH: ubiquinone-6 oxidoreductase has been sequenced. The DNA sequence indicates the presence of an open reading frame of 1539 bp predicted to encode a protein of 513 amino acid residues (57.2 kDa). The NADH dehydrogenase is synthesized as a precursor protein containing a signal sequence of 26 residues. In vitro import experiments show that the precursor NADH dehydrogenase is cleaved to the mature size by the matrix processing peptidase. Both cleavage and translocation across the mitochondrial membrane(s) are dependent on the membrane potential component of the proton-motive force. Comparison of the protein sequence of the yeast NADH dehydrogenase with the data bank indicates that the enzyme from yeast is homologous to the NADH dehydrogenase of Escherichia coli (22.2% identical residues). Both NADH dehydrogenases contain in the central part of the protein a sequence predicted to fold into a βαβ structure involved in the binding of NADH or FAD(H2). Various aspects of the protein structure are discussed.