R. Ferreira et al., Cell cycle-dependent recruitment of HDAC-1 correlates with deacetylation of histone H4 on an Rb-E2F target promoter, EMBO REP, 2(9), 2001, pp. 794-799
The transcription factor E2F, which is a key element in the control of cell
proliferation, is repressed by Rb and other pocket proteins in growth-arre
sted differentiating cells, as well as in proliferating cells when they pro
gress through early G(1). It is not known whether similar mechanisms are op
erative in the two situations. A body of data suggests that E2F repression
by pocket proteins involves class I histone deacetylases (HDACs). It has be
en hypothesized that these enzymes are recruited to E2F target promoters wh
ere they deacetylate histones. Here we have tested this hypothesis directly
by using formaldehyde cross-linked chromatin immunoprecipitation (XChIP) a
ssays to evaluate HDAC association in living cells. Our data show that a hi
stone deacetylase, HDAC-1, is stably bound to an E2F target promoter during
early G, in proliferating cells and released at the G(1)-S transition. In
addition, our results reveal an inverse correlation between HDAC-1 recruitm
ent and histone H4 acetylation on specific lysines.