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BMC Struct Biol. 2014 Jan 14;14:2. doi: 10.1186/1472-6807-14-2.

Dimeric structure of p300/CBP associated factor.

Author information

1
State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen 361102, China. jhan@xmu.edu.cn.

Abstract

BACKGROUND:

p300/CBP associating factor (PCAF, also known as KAT2B for lysine acetyltransferase 2B) is a catalytic subunit of megadalton metazoan complex ATAC (Ada-Two-A containing complex) for acetylation of histones. However, relatively little is known about the regulation of the enzymatic activity of PCAF.

RESULTS:

Here we present two dimeric structures of the PCAF acetyltransferase (HAT) domain. These dimerizations are mediated by either four-helical hydrophobic interactions or a ß-sheet extension. Our chemical cross-linking experiments in combined with site-directed mutagenesis demonstrated that the PCAF HAT domain mainly forms a dimer in solution through one of the observed interfaces. The results of maltose binding protein (MBP)-pulldown, co-immunoprecipitation and multiangle static light scattering experiments further indicated that PCAF dimeric state is detectable and may possibly exist in vivo.

CONCLUSIONS:

Taken together, our structural and biochemical studies indicate that PCAF appears to be a dimer in its functional ATAC complex.

PMID:
24423233
PMCID:
PMC3897949
DOI:
10.1186/1472-6807-14-2
[Indexed for MEDLINE]
Free PMC Article

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