Isolation and nucleotide sequence of the Saccharomyces cerevisiae gene for the succinate dehydrogenase flavoprotein subunit

• Published in: The Journal of biological chemistry Vol. 267; no. 14; pp. 10101 - 10107
• Main Authors: Robinson, K.M. (University of Alberta, Edmonton, Alberta, Canada), Lemire, B.D
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 15-05-1992
• Subjects: Amino Acid Sequence; Base Sequence; Biological and medical sciences; Blotting, Western; Chromosome Mapping; Chromosomes, Fungal; Cloning, Molecular; DNA, Fungal - genetics; DNA, Fungal - isolation & purification; Flavoproteins - genetics; Flavoproteins - isolation & purification; Flavoproteins - metabolism; Fundamental and applied biological sciences. Psychology; GENE; GENES; Genes, Fungal; Genes. Genome; inner membranes; Macromolecular Substances; mitochondria; Mitochondria - enzymology; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; NUCLEOTIDE; nucleotide sequence; NUCLEOTIDOS; Polymerase Chain Reaction - methods; predictions; Restriction Mapping; SACCHAROMYCES CEREVISIAE; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - genetics; Sequence Homology, Nucleic Acid; succinate dehydrogenase; Succinate Dehydrogenase - genetics; Succinate Dehydrogenase - isolation & purification; Succinate Dehydrogenase - metabolism; SUCCINATE DESHYDROGENASE; SUCINATO DESHIDROGENASA; Succinate dehydrogenase; Yeast; Nucleotide sequence; Enzyme; Fungi; Mitochondria; Gene; Membrane transport; Isolation; Ascomycetes; Molecular cloning; Saccharomyces cerevisiae; Aminoacid sequence; Thallophyta
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(19)50205-8

Succinate dehydrogenase (EC 1.3.99.1) of the mitochondrial inner membrane is a four-subunit membrane-bound enzyme that catalyzes the oxidation of succinate to fumarate and the transfer of electrons into the electron transport chain to oxygen. The catalytic domain of the enzyme is composed of a flavoprotein subunit which contains a covalently attached FAD cofactor and an iron-sulfur subunit with three nonidentical iron-sulfur clusters. We have isolated a complete genomic clone for the flavoprotein subunit of the succinate dehydrogenase from Saccharomyces cerevisiae and determined its nucleotide sequence. The sequence predicts a protein of 70,185 Da (640 amino acids) that shows more similarity to the Escherichia coli succinate dehydrogenase flavoprotein subunit than it does to the only other mitochondrial homologue, the human flavoprotein subunit. The yeast flavoprotein subunit precursor was synthesized in a cell-free translation system and shown to possess a mitochondrial targeting sequence that directs its import into isolated, energized mitochondria where it is processed by the matrix-localized protease. The genes for the flavoprotein and the iron-sulfur subunits reside on different chromosomes and hence form different transcriptional units