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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondrially encoded protein. Braun, H.P., Schmitz, U.K. FEBS Lett. (1993) [Pubmed]
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