Document Detail


Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription.
MedLine Citation:
PMID:  18258596     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Linker histone H1 has been generally viewed as a global repressor of transcription by preventing the access of transcription factors to sites in chromatin. However, recent studies suggest that H1 can interact with other regulatory factors for its action as a negative modulator of specific genes. To investigate these aspects, we established a human cell line expressing H1.2, one of the H1 subtypes, for the purification of H1-interacting proteins. Our results showed that H1.2 can stably associate with sets of cofactors and ribosomal proteins that can significantly repress p53-dependent, p300-mediated chromatin transcription. This repressive action of H1.2 complex involves direct interaction of H1.2 with p53, which in turn blocks p300-mediated acetylation of chromatin. YB1 and PURalpha, two factors present in the H1.2 complex, together with H1.2 can closely recapitulate the repressive action of the entire H1.2 complex in transcription. Chromatin immunoprecipitation and RNA interference analyses further confirmed that the recruitment of YB1, PURalpha, and H1.2 to the p53 target gene Bax is required for repression of p53-induced transcription. Therefore, these results reveal a previously unrecognized function of H1 as a transcriptional repressor as well as the underlying mechanism involving specific sets of factors in this repression process.
Authors:
Kyunghwan Kim; Jongkyu Choi; Kyu Heo; Hyunjung Kim; David Levens; Kimitoshi Kohno; Edward M Johnson; Hugh W Brock; Woojin An
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-02-07
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  283     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2008 Apr 
Date Detail:
Created Date:  2008-03-31     Completed Date:  2008-05-22     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  9113-26     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, University of Southern California Keck School of Medicine, Los Angeles, CA 90089, USA.
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MeSH Terms
Descriptor/Qualifier:
Acetylation
Chromatin / metabolism*
DNA-Binding Proteins / metabolism
E1A-Associated p300 Protein / metabolism
Gene Expression Regulation / physiology,  radiation effects*
Hela Cells
Histones / metabolism*
Humans
Nuclear Proteins / metabolism
RNA Interference
Repressor Proteins / metabolism*
Transcription Factors / metabolism
Transcription, Genetic / physiology*
Tumor Suppressor Protein p53 / metabolism*
bcl-2-Associated X Protein / biosynthesis
Chemical
Reg. No./Substance:
0/BAX protein, human; 0/Chromatin; 0/DNA-Binding Proteins; 0/Histones; 0/Nuclear Proteins; 0/PURA protein, human; 0/Repressor Proteins; 0/TP53 protein, human; 0/Transcription Factors; 0/Tumor Suppressor Protein p53; 0/YBX1 protein, human; 0/bcl-2-Associated X Protein; EC 2.3.1.48/E1A-Associated p300 Protein; EC 2.3.1.48/EP300 protein, human
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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