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

FEBS Letters

Schmitz, Udo K.¹  Braun, Hans-Peter¹ 

[1] Institut für Genbiologische Forschung Berlin GmbH, Ihnestrasse 63, W-1000 Berlin 33, Germany

关键词: Mitochondria;    Cytochrome c reductase;    Cytochrome b;    Methionine aminopeptidase;    Solanum tuberosum;    cox;    cytochrome c oxidase;    ND;    NADH dehydrogenase;    ATPase;    F0F1-ATPase/synthase;   

DOI  :  10.1016/0014-5793(93)81200-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown