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Dimeric structure of p300/CBP associated factor.

Shasha Shi, Juanyu Lin, Yongfei Cai

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

BMC Structural Biology
|January 16, 2014
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Summary
This summary is machine-generated.

The p300/CBP associating factor (PCAF) acetyltransferase domain primarily exists as a dimer. Structural and biochemical data suggest this dimerization is crucial for its function within the ATAC complex.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • PCAF (lysine acetyltransferase 2B) is a key component of the ATAC complex, involved in histone acetylation.
  • Regulation of PCAF's enzymatic activity remains poorly understood.

Purpose of the Study:

  • To elucidate the structural basis of PCAF's regulation.
  • To investigate the oligomeric state of the PCAF HAT domain.

Main Methods:

  • X-ray crystallography to determine dimeric structures.
  • Chemical cross-linking and site-directed mutagenesis.
  • MBP-pulldown, co-immunoprecipitation, and multiangle static light scattering.

Main Results:

  • Two distinct dimeric structures of the PCAF HAT domain were resolved, involving four-helical or ß-sheet interactions.
  • PCAF HAT domain predominantly dimerizes in solution via a specific interface.
  • Evidence suggests PCAF exists in a dimeric state in vivo.

Conclusions:

  • PCAF functions as a dimer within the ATAC complex.
  • Structural and biochemical data support PCAF dimerization as functionally relevant.