Journal
FEBS LETTERS
Volume 582, Issue 10, Pages 1501-1507Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.03.044
Keywords
peptide transduction; acetyl-histone tail; bromodomain; Brd4; FRAP
Funding
- Intramural NIH HHS [Z99 HD999999, Z01 HD008815-01] Funding Source: Medline
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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. Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.
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