CiteULike is a free online bibliography manager. Register and you can start organising your references online.

Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Export

Proceedings of the National Academy of Sciences of the United States of America, Vol. 105, No. 26. (1 July 2008), pp. 9000-9005.

Citation Format

[Posts]

View FullText article


caseybrown's tags for this article

hdac

X Reviews [Write a review of this article]

X Find related articles from these CiteULike users

X Find related articles with these CiteULike tags

X Posting History

X Abstract

Promoter chromatin disassembly is a widely used mechanism to regulate eukaryotic transcriptional induction. Delaying histone H3/H4 removal from the yeast PHO5 promoter also leads to delayed removal of histones H2A/H2B, suggesting a constant equilibrium of assembly and disassembly of H2A/H2B, whereas H3/H4 disassembly is the highly regulated step. Toward understanding how H3/H4 disassembly is regulated, we observe a drastic increase in the levels of histone H3 acetylated on lysine-56 (K56ac) during promoter chromatin disassembly. Indeed, promoter chromatin disassembly is driven by Rtt109 and Asf1-dependent acetylation of H3 K56. Conversely, promoter chromatin reassembly during transcriptional repression is accompanied by decreased levels of histone H3 acetylated on lysine-56, and a mutation that prevents K56 acetylation increases the rate of transcriptional repression. As such, H3 K56 acetylation drives chromatin toward the disassembled state during transcriptional activation, whereas loss of H3 K56 acetylation drives the chromatin toward the assembled state.


X BibTeX record

X RIS record


Privacy Statement | Terms & Conditions
CiteULike organises scholarly (or academic) papers or literature and provides bibliographic (which means it makes bibliographies) for universities and higher education establishments. It helps undergraduates and postgraduates. People studying for PhDs or in postdoctoral (postdoc) positions. The service is similar in scope to EndNote or RefWorks or any other reference manager like BibTeX, but it is a social bookmarking service for scientists and humanities researchers.