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CtBP represses p300-mediated transcriptional activation by direct association with its bromodomain

Cited 83 time in Web of Science Cited 84 time in Scopus
Authors
Kim, Jae-Hwan; Cho, Eun-Jung; Kim, Seong-Tae; Youn, HOng-Duk
Issue Date
2005-04-19
Publisher
Nature Publishing Group
Citation
Nat Struct Mol Biol. 2005 May;12(5):423-8. Epub 2005 Apr 17.
Keywords
Acetyltransferases/*chemistry/*metabolismAlcohol OxidoreductasesAmino Acid SequenceAnimalsBinding, CompetitiveCell Cycle Proteins/*chemistry/*metabolismCell LineDNA-Binding Proteins/chemistry/genetics/*metabolismHistone AcetyltransferasesHistones/metabolismHumansMiceMice, KnockoutMolecular Sequence DataMutation/geneticsNAD/metabolismPhosphoproteins/chemistry/genetics/*metabolismProtein BindingProtein Structure, TertiaryRepressor Proteins/chemistry/genetics/metabolismSequence AlignmentTranscription Factors/*chemistry/*metabolismTranscriptional Activation/*geneticsp300-CBP Transcription Factors
Abstract
Histone acetyltransferase coactivators bind to acetylated histones through their bromodomains and catalyze the acetylation of histone H3 and H4 tails for transcriptional activation. C-terminal binding protein (CtBP) serves as a transcriptional corepressor by recruiting histone deacetylases. However, the precise mechanism by which CtBP represses transcription has not been determined. In this study we found that CtBP1 directly associates with p300 by binding to the PXDLS motif in the bromodomain of p300. Moreover, CtBP1 blocks the accessibility of p300 to histones in an NADH-sensitive manner and thus represses p300-mediated histone acetylation and transcriptional activation. In addition, an NADH-nonresponsive, monomeric mutant, CtBP1 (G183V), was found to strongly repress p300-mediated transcriptional activation. Thus, the dissociation of NADH from CtBP1 leads to the repression of p300-driven general transcriptional activity by CtBP1. These results suggest a novel mechanism whereby CtBP1 serves as an energy-sensing repressor of histone acetyltransferase(s) and thus affects general transcription.
ISSN
1545-9993 (Print)
Language
English
URI
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15834423

http://hdl.handle.net/10371/29035
DOI
https://doi.org/10.1038/nsmb924
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Biochemistry & Molecular Biology (생화학교실)Journal Papers (저널논문_생화학교실)
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