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)