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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nishiyama A,Mochizuki K,Mueller F,Karpova T,McNally JG,Ozato Kdoi
10.1016/j.febslet.2008.03.044subject
Has Abstractpub_date
2008-04-30 00:00:00pages
1501-7issue
10eissn
0014-5793issn
1873-3468pii
S0014-5793(08)00291-3journal_volume
582pub_type
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