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The primary structure of histone H3 from the nematode Caenorhabditis elegans


, : The primary structure of histone H3 from the nematode Caenorhabditis elegans. FEBS Letters 211(1): 59-63

The complete primary structure of histone H2A from the nematode C. elegans was determined. The amino acid chain consisted of 126 amino acid residues and had a blocked N-terminus in comparison with calf thymus histone H2A, the nematode protein showed 5 deletions, 2 insertions and 16 substitutions. Most of the changes occur in the N- and C-terminal regions of the molecule, whereas the central part covering the residues 21-120 was quite well conserved. The lysine residues 5, 8 and 10 were partially acetylated.

Accession: 001714079

PMID: 3606579

DOI: 10.1042/bj2430297

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Related references

Vanfleteren, J.R.; Van Bun, S.M.; Van Beeumen, J.J., 1987: The primary structure of histone H2A from the nematode Caenorhabditis elegans. The complete amino acid sequence of histone H3 (135 residues) from the nematode Caenorhabditis elegans has been established. Microheterogeneity occurs at positions 96 and 100 of the chain. The sequences of the nematode H3 isoforms are very similar...

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