Ra. Swank et al., 4 DISTINCT CYCLIN-DEPENDENT KINASES PHOSPHORYLATE HISTONE H1 AT ALL OF ITS GROWTH-RELATED PHOSPHORYLATION SITES, Biochemistry, 36(45), 1997, pp. 13761-13768
In mammalian cells, up to six serines and threonines in histone H1 are
phosphorylated in vivo in a cell cycle dependent manner that has long
been linked with chromatin condensation. Growth-associated H1 kinases
, now known as cyclin-dependent kinases (CDKs), are thought to be the
enzymes responsible for this process. This paper describes the phospho
rylation of histone H1 by four different purified CDKs. The four CDKs
phosphorylate only the cell cycle specific phosphorylation sites of H1
, indicating that they belong to the kinase class responsible for grow
th-related H1 phosphorylation in vivo. All four CDKs phosphorylate all
of the interphase and mitotic-specific H1 sites. In addition to the (
S/T)PXK consensus phosphorylation sires, these four CDKs also phosphor
ylate a mitotic-specific in vivo H1 phosphorylation site that lacks th
is sequence. There is no site selectivity among the growth-related pho
sphorylation sites by any of the four CDKs because all four CDKs phosp
horylate all relevant sites. The results imply that the cell cycle dep
endent H1 phosphorylations observed in vivo must involve differential
accessibility of H1 sites at different stages of the cell cycle.