Primary structure, import, and assembly of the yeast homolog of succinate dehydrogenase flavoprotein.
We have isolated a homolog for the flavoprotein subunit of succinate dehydrogenase [succinate:(acceptor) oxidoreductase, EC 1.3.99.1] from Saccharomyces cerevisiae and used the obtained peptide sequences to clone and characterize the corresponding gene. It contained an open reading frame of 1923 base pairs and encoded a protein of 640 amino acids (M(r), 70,238) that showed approximately 49% and approximately 28% identity with the Escherichia coli and Bacillus subtilis enzymes, respectively. All features of the FAD cofactor binding site were completely conserved. Comparison of the deduced protein sequence with the N-terminal sequence determined from the isolated protein revealed an N-terminal extension of 28 amino acids that presumably represents a mitochondrial signal sequence. After in vitro transcription and translation, the preprotein was efficiently imported into isolated yeast mitochondria, cleaved to its mature form, and assembled into the membrane-bound succinate dehydrogenase complex.
Schülke
N
N
Rockefeller University, Laboratory of Cell Biology, Howard Hughes Medical Institute, New York, NY 10021.
Blobel
G
G
Pain
D
D
D000595:Amino Acid Sequence; D001483:Base Sequence; D001692:Biological Transport; D002451:Cell Compartmentation; D003001:Cloning, Molecular; D005800:Genes, Fungal; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D016133:Polymerase Chain Reaction; D011498:Protein Precursors / Q000378:metabolism; D016415:Sequence Alignment; D013385:Succinate Dehydrogenase / Q000737:chemistry / Q000378:metabolism*
D009838:Oligodeoxyribonucleotides; D011498:Protein Precursors; D013385:Succinate Dehydrogenase