A TPR motif cofactor contributes to p300 activity in the p53 response

Demonacos, C., Krstic-Demonacos, M. and La Thangue, N.B. (2001) A TPR motif cofactor contributes to p300 activity in the p53 response. Molecular Cell, 8, pp. 71-84.

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Abstract

The transcription of p53 target genes involves p300/CBP coactivators, which are multiprotein complexes that interact with the p53 activation domain. We report a cofactor in the p300 coactivator complex, Strap, which has an unusual structure, being composed almost entirely of a tandem series of six tetratricopeptide repeat (TPR) motifs. The TPR motif functions as a protein interaction domain, and it is consistent with this property that Strap harbors distinct and dedicated domains that allow it to bind and augment the interaction between different components of the p300 complex. Strap facilitates p53 activity in response to stress, in part through the stress-responsive accumulation of Strap protein and interfering with the MDM2-dependent downregulation of p53.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Krstic-Demonacos, Dr Marija
Authors: Demonacos, C., Krstic-Demonacos, M., and La Thangue, N.B.
College/School:College of Medical Veterinary and Life Sciences
Journal Name:Molecular Cell

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