Open AccessThe primary structure of cytochrome c 1 from Neurospora crassa
Author(s) -
RÖMISCH Jürgen,
TROPSCHUG Maximilian,
SEBALD Walter,
WEISS Hanns
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb11000.x
Subject(s) - neurospora crassa , protein primary structure , biochemistry , cytochrome , amino acid , cytochrome c1 , protein subunit , complementary dna , peptide sequence , neurospora , cytochrome b , cytochrome c oxidase , chemistry , biology , hemeprotein , heme , cytochrome c , stereochemistry , mitochondrion , coenzyme q – cytochrome c reductase , gene , enzyme , mitochondrial dna , mutant
The primary structure of the cytochrome c 1 subunit of ubiquinol‐cytochrome‐ c reductase from mitochondria of Neurospora crassa was determined by sequencing the cDNA of a bank cloned in Escherichia coli . From the coding region the sequence of 332 amino acids, corresponding to the molecular mass of 36496 Da, was derived for the precursor protein. The mature protein, the N terminus of which was previously sequenced [Tsugita et al. (1979) in Cytochrome oxidase (King, T. E. et al., eds) pp. 67–77, Elsevier, New York], consists of 262 amino acids and has the molecular mass of 29 908 Da including the heme. The sequence contains an N‐terminal hydrophilic part of 211 residues, which carries the heme, a hydrophobic stretch of 15 residues, which is assumed to anchor the protein to the membrane, and a C‐terminal hydrophilic part of 36 residues. The N‐terminal presequence of 70 amino acids contains 9 positive charges but only 1 negative charge and is characterized by a stretch of 20 uncharged residues.