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Synergistic action of MLL, a TRX protein with template activating factor‐I, a histone chaperone
Author(s) -
Shimoyama Tae,
Kato Kohsuke,
Miyaji-Yamaguchi Mary,
Nagata Kyosuke
Publication year - 2005
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.2004.12.064
Subject(s) - chromatin immunoprecipitation , histone , chromatin , transcription factor , microbiology and biotechnology , transcription (linguistics) , chaperone (clinical) , chemistry , dna binding protein , promoter , biology , gene , biochemistry , gene expression , medicine , linguistics , philosophy , pathology
MLL is involved in the process of gene activity maintenance. It is shown that the amino‐terminal region of MLL (MLLN) interacts with TAF‐Iβ/SET. In this study, using yeast two‐hybrid assays, we have found that the acidic region of TAF‐Iβ is essential for its binding to MLLN. Pull‐down assays using GST‐MLLN demonstrated that TAF‐Iβ and histones interact with GST‐MLLN. MLLN and TAF‐Iβ synergistically upregulated the transcription level of Hoxa9 and co‐immunoprecipitated in chromatin containing the Hoxa9 promoter region. These results suggest that TAF‐Iβ plays an important role in MLL‐mediated transcription and possibly chromatin maintenance.