Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF (Cell, 121:873-885, 17 June 2005)

報告日期: 2005/11/01
報告時間: 17:10/18:00
報告學生: 莊健盈
講評老師: 陳炳焜
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Physical Association and Coordinate Function of the H3 K4 Methyltransferase MLL1 and the H4 K16 Acetyltransferase MOF

Yali Dou, Thomas A. Milne, Alan J. Tackett, Edwin R. Smith, Aya Fukuda, Joanna Wysocka, C. David Allis, Brian T. Chait, Jay L. Hess, and Robert G. Roeder                                         Cell, 2005, Vol. 121, 873-885

 

Speaker: 莊健盈                            Time: 1/11/2005 17:10~18:10

Commentator: 陳炳焜 老師                   Place: Room 602

 

Abstract:

 

  The lysine methylation of histone is recognized as an important epigenetic regulation of eukaryotes gene expression. For example, methylation of lysine (K4) of histone H3 has been linked to transcriptional activation in a variety of eukaryotes. MLL1 (mixed-lineage leukemia) is capable of methylating H3 at K4 and regulates p27, p18, and Hox genes expression. To understand the function and mechanism of MLL1 H3 K4 methyltransferase activity in transcriptional regulation, the author used an immunoaffinity purification assay to find some association proteins of the MLL1, such as MOF, Ring2, RbBP5, and Ash2L. In this paper, the interaction between MLL1 and MOF was confirmed by coimmunoprecipitation, and interacted domains were mapped to MLL1 C-terminal and MOF zinc finger regions. In addition, they identified that the MLL1 complex (MLL1, MOF, WDR5, Ring2, RbBP5, and Ash2L) has H3 K4-specific HMT and H4 K16-specific HAT activities, and both activities are required for optimal transcription activity on a MLL target gene in vivo and on a chromatin template in vitro. These results lead to a model for both the establishment and spreading of H3 K4 methylation, perhaps in conjunction with H4 K16 acetylation, in transcription active chromatin.

 

References:

 

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