Intracellular delivery of acetyl-histone peptides inhibits native bromodomain-chromatin interactions and impairs mitotic progression

  • Nishiyama A
  • Mochizuki K
  • Mueller F
 et al. 
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Abstract

Bromodomains present in Brd4 and other chromatin proteins interact with acetylated histones to regulate transcription and cell growth. To study Brd4-chromatin interactions in vivo, histone H4 tail peptides were fused to a synthetic protein transduction domain (PTD) derived from the human immunodeficiency virus Tat and delivered into cultured cells. Acetyl-H4 peptides, but not unacetylated H4 peptides inhibited real time Brd4-chromatin interactions in living cells as assessed by fluorescence recovery after photobleaching assays. The acetyl-H4 peptides also inhibited an interaction of Brd4 with chromosomes during mitosis and reduced cell growth potential. Together, PTD-based delivery of histone tail peptides offers a novel means to study the mechanism and biological significance of bromodomain-chromatin interactions in vivo.

Author-supplied keywords

  • Acetyl-histone tail
  • Brd4
  • Bromodomain
  • FRAP
  • Peptide transduction

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Authors

  • Akira Nishiyama

  • Kazuki Mochizuki

  • Florian Mueller

  • Tatiana Karpova

  • James G. McNally

  • Keiko Ozato

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