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Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation.

Abstract：

:Lysine acetylation of the tumor suppressor protein p53 in response to a wide variety of cellular stress signals is required for its activation as a transcription factor that regulates cell cycle arrest, senescence, or apoptosis. Here, we report that the conserved bromo-domain of the transcriptional coactivator CBP (CREB binding protein) binds specifically to p53 at the C-terminal acetylated lysine 382. This bromodomain/acetyl-lysine binding is responsible for p53 acetylation-dependent coactivator recruitment after DNA damage, a step essential for p53-induced transcriptional activation of the cyclin-dependent kinase inhibitor p21 in G1 cell cycle arrest. We further present the three-dimensional nuclear magnetic resonance structure of the CBP bromodomain in complex with a lysine 382-acetylated p53 peptide. Using structural and biochemical analyses, we define the molecular determinants for the specificity of this molecular recognition.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Mujtaba S,He Y,Zeng L,Yan S,Plotnikova O,Sachchidanand,Sanchez R,Zeleznik-Le NJ,Ronai Z,Zhou MM

doi

10.1016/s1097-2765(03)00528-8

subject

Has Abstract

pub_date

2004-01-30 00:00:00

pages

251-63

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(03)00528-8

journal_volume

13

pub_type

杂志文章

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