Premium
Characterization of the Phosphoryl‐Nitrogen Linkages in Histone H4
Author(s) -
Bruegger B. B.,
Delange R. J.,
Smith R. A.,
Lin Y. C.
Publication year - 1979
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.197900002
Subject(s) - chemistry , enzyme , histone , biochemistry , phosphorylation , histidine , lysine , kinase , histone h4 , amino acid , dna
In earlier work we nave described and partially characterized two histone kinases from regenerating rat liver and other tissues which catalyze the transfer of the γ‐phosphoryl group from ATP to histones. The histone phosphates thus formed were observed to be acid‐labile and base‐stable. In the present study we report on the specificity of one of these enzymes, namely, the kinase which is optimally active at pH 9. This enzyme appears to be relatively specific for the two histidine residues of histone H4. These histidines occur at positions 18 and 75, and both are phosphorylated. However, when regenerating rat liver was the source of enzyme, the product was 1‐phosphohistidine, whereas the enzyme from Walker‐256 carcinosarcoma catalyzed the formation of 3‐phosphohistidine.