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. 1987 Apr 1;243(1):297–300. doi: 10.1042/bj2430297

The primary structure of histone H2A from the nematode Caenorhabditis elegans.

J R Vanfleteren, S M Van Bun, J J Van Beeumen
PMCID: PMC1147849  PMID: 3606579

Abstract

The complete primary structure of histone H2A from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 126 amino acid residues and has a blocked N-terminus. By comparison with calf thymus histone H2A, the nematode protein shows five deletions, two 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 is quite well conserved. The lysine residues 5, 8 and 10 were found to be partially acetylated.

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Selected References

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