PURIFICATION AND SEQUENCING OF CYTOCHROME-B FROM POTATO REVEALS METHIONINE CLEAVAGE OF A MITOCHONDRIALLY ENCODED PROTEIN

被引：19

作者：

BRAUN, HP ^{[1
]}

SCHMITZ, UK ^{[1
]}

机构：

[1] FORSCHUNG BERLIN GMBH,INST GENBIOL,IHNESTR 63,W-1000 BERLIN 33,GERMANY

来源：

FEBS LETTERS | 1993年 / 316卷 / 02期

关键词：

MITOCHONDRIA; CYTOCHROME-C REDUCTASE; CYTOCHROME-B; METHIONINE AMINOPEPTIDASE; SOLANUM-TUBEROSUM;

D O I：

10.1016/0014-5793(93)81200-J

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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-formylmethionine is removed. This result provides the first evidence for the presence of a deformylase and a methionine aminopeptidase in mitochondria.

引用

页码：128 / 132

页数：5

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