Premium
Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondriallly encoded protein
Author(s) -
Braun Hans-Peter,
Schmitz Udo K.
Publication year - 1993
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(93)81200-j
Subject(s) - methionine , biochemistry , cytochrome b , cytochrome , biology , mitochondrion , gene , amino acid , cytochrome c , peptide sequence , microbiology and biotechnology , mitochondrial dna , enzyme
Several mitochondrial genes from a large number of different fungi, mammals and plants have been sequenced but little is known about the corresponding translation products. We have affinity purified cytochrome c reductase from potato mitochondria and isolated the mitochondrially encoded cytochrome b protein. Amino‐terminal sequencing reveals that the polypeptide does not start with a methionine. Comparison of the amino acid sequence with the recently published sequence of the gene encoding the cytochrome b apoprotein suggests that the N ‐fonnylmetnionine is removed. This result provides the first evidence for the presence of a deformylase and a methionine aminopeptidase in mitochondria.