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A Novel Modification of the Lysine Residue at Position 12 of Histone H4 in Starfish Sperm
K Nunomura1, T Shimizu1, K Hozumi1
1a Department of Applied Biochemistry , Hiroshima University , 1-4-4 Kagamiyama, Higashi-hiroshima, Hiroshima 739 , Japan.
Abstract:
Post-translational modification of core histones is essential in processes requiring chromatin remodeling. We report here a novel modification in histones of the sperm of the starfish, Asterina pectinifera, which involves an ε-(γ-glutamyl)lysine cross-link between the glutamine residue at position 9 of histone H2B and the lysine residue at position 12 of histone H4.
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