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

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  • Max Planck Institute of Molecular Plant Physiology (MPI-MP)
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Original languageEnglish
Pages (from-to)128-132
Number of pages5
JournalFEBS letters
Volume316
Issue number2
Publication statusPublished - 25 Jan 1993
Externally publishedYes

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.

Keywords

    Cytochrome b, Cytochrome c reductase, Methionine aminopeptidase, Mitochondria, Solanum tuberosum

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Cite this

Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondriallly encoded protein. / Braun, Hans-Peter; Schmitz, Udo.
In: FEBS letters, Vol. 316, No. 2, 25.01.1993, p. 128-132.

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AU - Braun, Hans-Peter

AU - Schmitz, Udo

N1 - Funding information: AcknowledgemenWtse: are greatlyi ndeptedt o Dr. V. Kruft, Berlin, for sequencingth e cytochromeb protein.W e wish to thankP rof. G. Schatz,B asel,w ho madea ntibodiesa gainstc ytochromebs from yeast available to us. This work was supported by the Deutsche Forschungsgemeinscha(Sftc hm6 98/2-2).

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N2 - 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.

AB - 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.

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