The phosphorylation region of lysine-rich histone in dividing cells

N-Bromosuccinimide cleavage of in vivo ³²P-labelled lysine-rich histone isolated from rapidly dividing cells has been studied. N-Bromosuccinimide cleaves F₁-histone into two fragments, a small N-terminal piece and a larger C-terminal portion. The phosphate-induced microheterogeneity and associated radioactivity which has been linked to cell replication, is found in the carboxyterminal fragment. No phosphorous is found associated with the amino-terminal fragment when histone phosphorylation is associated with cell division. The specific tryptic phosphopeptides obtained from in vivo labelled F₁ are clearly different from those obtained from in vitro incubations of free F₁-histone and cytoplasmic protein kinase.