Ligand activation of Notch leads to the release of Notch IC (the intracellular receptor domain), which translocates to the nucleus and interacts with the DNA-binding protein CSL to control expression of specific target genes. In addition to ligand-mediated activation, Notch signalling can be further modulated by interactions of Notch IC with a number of other proteins. MAML1 has previously been shown to act co-operatively with the histone acetyltransferase p300 in Notch IC-mediated transcription. In the present study we show that the N-terminal domain of MAML1 directly interacts with both p300 and histones, and the p300–MAML1 complex specifically acetylates histone H3 and H4 tails in chromatin. Furthermore, p300 acetylates MAML1 and evolutionarily conserved lysine residues in the MAML1 N-terminus are direct substrates for p300-mediated acetylation. The N-terminal domain of MAML1 contains a proline repeat motif (PXPAAPAP) that was previously shown to be present in p53 and important for the p300–p53 interaction. We show that the MAML1 proline repeat motif interacts with p300 and enhances the activity of the MAML1 N-terminus in vivo. These findings suggest that the N-terminal domain of MAML1 plays an important role in Notch-regulated transcription, by direct interactions with Notch, p300 and histones.
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Research Article|
May 14 2007
A proline repeat domain in the Notch co-activator MAML1 is important for the p300-mediated acetylation of MAML1
Mariana Saint Just Ribeiro;
Mariana Saint Just Ribeiro
1Department of Biosciences and Nutrition, Karolinska Institutet, 141 86 Stockholm, Sweden
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Magnus L. Hansson;
Magnus L. Hansson
1Department of Biosciences and Nutrition, Karolinska Institutet, 141 86 Stockholm, Sweden
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Annika E. Wallberg
Annika E. Wallberg
1
1Department of Biosciences and Nutrition, Karolinska Institutet, 141 86 Stockholm, Sweden
1To whom correspondence should be addressed (email annika.wallberg@mednut.ki.se).
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Publisher: Portland Press Ltd
Received:
December 20 2006
Accepted:
February 14 2007
Accepted Manuscript online:
February 14 2007
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2007 Biochemical Society
2007
Biochem J (2007) 404 (2): 289–298.
Article history
Received:
December 20 2006
Accepted:
February 14 2007
Accepted Manuscript online:
February 14 2007
Citation
Mariana Saint Just Ribeiro, Magnus L. Hansson, Annika E. Wallberg; A proline repeat domain in the Notch co-activator MAML1 is important for the p300-mediated acetylation of MAML1. Biochem J 1 June 2007; 404 (2): 289–298. doi: https://doi.org/10.1042/BJ20061900
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