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Relationship between a subunit of NADH dehydrogenase (complex I) and a protein family including subunits of cytochrome reductase and processing protease of mitochondria
Author(s) -
D. A. Röhlen,
Jan Hoffmann,
Jakub Paś,
Uwe Nehls,
Dagmar Preis,
U. Sackmann,
Hanns Weiss
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80087-j
Subject(s) - biochemistry , protein subunit , biology , nadh dehydrogenase , respiratory chain , neurospora crassa , mitochondrion , cytochrome c oxidase , reductase , mitochondrial matrix , peptide sequence , complementary dna , protein targeting , gene , enzyme , membrane protein , cytosol , membrane , mutant
The primanry structure of a 40 kDa subunit of the respiratory chain NADH:ubiquinone reductase from Neurospora crassa was determined by sequencing cDNA, genomic DNA and the N‐terminus of the mature protein. The gene which is interrupted by 7 introns encodes a preprotein consisting of 375 amino acids with a 26 amino acid long presequence typical for a mitochondrial targetting signal. The sequence of the mature subunit shows conspicuous similarities to the recently [(1989) Nature 339, 147–149] discovered protein family which includes subunits I and II of the ubiquinol:cytochrome c reductase, and the processing proteins, matrix processing peptidase and processing enhancing protein, of mitochondria. The possible role of the subunit is discussed.