title: The primary structure of histone H2A from the nematode Caenorhabditis elegans.
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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002107:Caenorhabditis / Q000032:analysis*; D002417:Cattle; D006657:Histones
chemical_list: D006657:Histones