Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae

Authors

  • Simon DE VRIES,

    Corresponding author
    1. Section for Molecular Biology and Biotechnology Centre, Department of Molecular Cell Biology, University of Amsterdam, The Netherlands
      Correspondence to Section for Molecular Biology, Department of Molecular Cell Biology, University of Amsterdam, Kruislaan 318, NL-1098 SM Amsterdam, The Netherlands.
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  • Richard VAN WITZENBURG,

    1. Section for Molecular Biology and Biotechnology Centre, Department of Molecular Cell Biology, University of Amsterdam, The Netherlands
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  • Leslie A. GRIVELL,

    1. Section for Molecular Biology and Biotechnology Centre, Department of Molecular Cell Biology, University of Amsterdam, The Netherlands
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  • Carla A. M. MARRES

    1. Section for Molecular Biology and Biotechnology Centre, Department of Molecular Cell Biology, University of Amsterdam, The Netherlands
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  • 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.

Correspondence to Section for Molecular Biology, Department of Molecular Cell Biology, University of Amsterdam, Kruislaan 318, NL-1098 SM Amsterdam, The Netherlands.

Abstract

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.

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