The primary structure of histone H2A from the nematode Caenorhabditis elegans
Keyword(s):
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.
2001 ◽
Vol 24
(1)
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pp. 14-18
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2005 ◽
Vol 280
(12)
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pp. 11025-11034
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2003 ◽
Vol 89
(4)
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pp. 778-790
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