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© Research
Publication : FEBS letters

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

Team: Imaging and Modeling
Team: Quantitative RNA imaging
Member: Florian Muller
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 07 Apr 2008

Nishiyama A, Mochizuki K, Mueller F, Karpova T, McNally JG, Ozato K

Link to Pubmed [PMID] – 18396160

FEBS Lett. 2008 Apr;582(10):1501-7

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.