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Vol. 16, No. 11, pp. 1397-1411, June 1, 2002
1 Regulatory Biology Laboratory and 2 Molecular
Neurobiology Laboratory, The Salk Institute for Biological Studies,
La Jolla, California 92037, USA
Signaling through the Notch pathway activates the proteolytic
release of the Notch intracellular domain (ICD), a dedicated transcriptional coactivator of CSL enhancer-binding proteins. Here we
show that chromatin-dependent transactivation by the recombinant Notch
ICD-CBF1 enhancer complex in vitro requires an additional coactivator,
Mastermind (MAM). MAM provides two activation domains necessary for
Notch signaling in mammalian cells and in Xenopus embryos. We
show that the central MAM activation domain (TAD1) recruits CBP/p300 to
promote nucleosome acetylation at Notch enhancers and activate
transcription in vitro. We also find that MAM expression induces
phosphorylation and relocalization of endogenous CBP/p300 proteins to
nuclear foci in vivo. Moreover, we show that coexpression with MAM and
CBF1 strongly enhances phosphorylation and proteolytic turnover of the
Notch ICD in vivo. Enhanced phosphorylation of the ICD and p300
requires a glutamine-rich region of MAM (TAD2) that is essential for
Notch transcription in vivo. Thus MAM may function as a timer to couple
transcription activation with disassembly of the Notch enhancer complex
on chromatin.
[Key Words: Notch; Mastermind; transcription activation; chromatin; phosphorylation; proteolysis]
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