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. 1990 Nov 1;271(3):613–620. doi: 10.1042/bj2710613

The primary structure of cytochrome c from the nematode Caenorhabditis elegans.

J R Vanfleteren 1, E A Evers 1, G Van de Werken 1, J J Van Beeumen 1
PMCID: PMC1149606  PMID: 2173902

Abstract

The complete amino acid sequence of cytochrome c from the nematode Caenorhabditis elegans was determined. The native protein displays the same spectral properties in the oxidized and reduced states as horse heart cytochrome c. The apoprotein consists of 110 amino acid residues and differs from human cytochrome c by 44 substitutions, one internal deletion, five N-terminal additions and two C-terminal additions. One of the substitutions is the replacement of an 'invariant' phenylalanine residue at position 15 by tyrosine. The N-terminal sequence extension contains a short peptide motif, which is highly homologous with a peptide fragment present at the N-terminus of annelid and insect cytochrome c sequences. From the number of amino acid changes and the evolutionary rate of cytochrome c it would appear that nematodes diverged from a line leading to man about 1.4 billion years ago. When similar data based on the amino acid sequences of the histones H1, H2A, H2B and H3 are taken into account, the average estimate is 1.1 +/- 0.1 billion years.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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