Dimeric structure of p300/CBP associated factor

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Humans
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Protein Conformation
  • Protein Multimerization
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • p300-CBP Transcription Factors / chemistry*
  • p300-CBP Transcription Factors / genetics
  • p300-CBP Transcription Factors / metabolism*

Substances

  • p300-CBP Transcription Factors
  • p300-CBP-associated factor

Associated data

  • PDB/4NSQ