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Regulation of histone acetyltransferase activity of p300 and PCAF by proto‐oncogene protein DEK
Author(s) -
Ko Soo-Il,
Lee In-Seon,
Kim Ji-Young,
Kim Sung-Mi,
Kim Dong-Wook,
Lee Kyu-Sun,
Woo Kyung-Mi,
Baek Jeong-Hwa,
Choo Jong-Kil,
Seo Sang-Beom
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.04.081
Subject(s) - histone acetyltransferase , pcaf , chromatin immunoprecipitation , bromodomain , p300 cbp transcription factors , histone , chromatin , acetylation , histone deacetylase 5 , sap30 , chemistry , microbiology and biotechnology , cancer research , biology , histone h2a , histone acetyltransferases , histone methyltransferase , promoter , biochemistry , gene expression , gene
The proto‐oncogene protein DEK has been implicated in the t(6;9) chromosomal translocation associated with a subtype of acute myelogenous leukemia (AML), which results in the formation of a DEK‐CAN fusion protein. Histone acetylation is an important post‐translational modification which is involved in transcriptional regulation. In this study, we report that the acidic domain containing protein DEK interacts with histones and exerts a potent inhibitory effect on both p300 and PCAF‐mediated histone acetyltransferase activity and transcription. Using chromatin immunoprecipitation assays, we have demonstrated that the recruitment of DEK to the appropriate promoter induces the histone H3 and H4 hypoacetylation of chromatin. Collectively, our data illustrate the important regulatory role played by protein DEK in transcriptional regulation, and suggest that transcription‐regulating acidic domain regions may play a role in leukemogenesis.