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PMID: 11073993 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Functional interaction between nucleosome assembly proteins and p300/CREB-binding protein family coactivators.

Molecular and cellular biology ·Vol. 20 ·No. 23 ·2000-12-00 ·Pages 8933-43

Shikama N, Chan HM, Krstic-Demonacos M, Smith L, Lee CW, Cairns W, La Thangue NB

Abstract

The p300/CREB-binding protein (CBP) family of proteins consists of coactivators that influence the activity of a wide variety of transcription factors. Although the mechanisms that allow p300/CBP proteins to achieve transcriptional control are not clear, it is believed that the regulation of chromatin is an important aspect of the process. Here, we describe a new level of p300-dependent control mediated through the functional interaction between p300/CBP and members of the family of nucleosome assembly proteins (NAP), which includes NAP1, NAP2, and TAF1. We find that NAP proteins, which have previously been implicated in the regulation of transcription factor binding to chromatin, augment the activity of different p300 targets, including p53 and E2F, through a process that is likely to involve the physical interaction between p300 and NAP. NAP proteins can form oligomers, and the results show that NAP proteins can bind to both core histones and p300 coactivator proteins, perhaps in a multicomponent ternary complex. We also provide data in support of the idea that histones can influence the interaction between p300 and NAP protein. These results argue that NAP is a functionally important component of the p300 coactivator complex and suggest that NAP may serve as a point of integration between transcriptional coactivators and chromatin.

MeSH Terms
Adenovirus E2 Proteins/metabolism Binding Sites CREB-Binding Protein Cell Cycle Proteins Chromosomal Proteins, Non-Histone DNA-Binding Proteins/metabolism Histone Chaperones Histones/metabolism Models, Genetic Nuclear Proteins/metabolism Nucleosome Assembly Protein 1 Nucleosomes/metabolism Protein Binding Protein Structure, Tertiary Proteins/metabolism Trans-Activators/metabolism Transcription Factors Transcription, Genetic Transcriptional Activation Tumor Suppressor Protein p53/metabolism
Chemicals
Adenovirus E2 Proteins Cell Cycle Proteins Chromosomal Proteins, Non-Histone DNA-Binding Proteins Histone Chaperones Histones NAP1L1 protein, human NAP1L4 protein, human Nuclear Proteins Nucleosome Assembly Protein 1 Nucleosomes Proteins SET protein, human Trans-Activators Transcription Factors Tumor Suppressor Protein p53 CREB-Binding Protein
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Shikama N
Division of Biochemistry and Molecular Biology, University of Glasgow, Glasgow G12 8QQ, United Kingdom.
Chan H M
Krstic-Demonacos M
Smith L
Lee C W
Cairns W
La Thangue N B
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.20.23.8933-8943.2000
Published
2000-12-00
Pages
8933-43
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC86548
Subset
IM
Grants
Wellcome Trust · United Kingdom
External Links
PubMed source DOI: 10.1128/MCB.20.23.8933-8943.2000 PMC Full Text View journal details
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