Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondriallly encoded protein

verfasst von
Hans-Peter Braun, Udo Schmitz
Abstract

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.

Externe Organisation(en)
Max-Planck-Institut für molekulare Pflanzenphysiologie
Typ
Artikel
Journal
FEBS letters
Band
316
Seiten
128-132
Anzahl der Seiten
5
ISSN
0014-5793
Publikationsdatum
25.01.1993
Publikationsstatus
Veröffentlicht
Peer-reviewed
Ja
ASJC Scopus Sachgebiete
Biophysik, Strukturelle Biologie, Biochemie, Molekularbiologie, Genetik, Zellbiologie
Elektronische Version(en)
https://doi.org/10.1016/0014-5793(93)81200-J (Zugang: Unbekannt)