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Ko, Myunggon
Molecular Immunology & Cancer Epigenetics
Research Interests
  • TET proteins, DNA hydroxymethylation, oncogenesis, cancer stem cells, cancer therapy

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Baf60a interacts with p53 to recruit the SWI/SNF complex

Cited 35 times inthomson ciCited 34 times inthomson ci
Title
Baf60a interacts with p53 to recruit the SWI/SNF complex
Author
Oh, JaehakSohn, Dong HKo, Myung GonChung, HeekyungJeon, SunghoSeong, Rho H
Keywords
Amines; Amino acids; Cell death; Flow interactions; Nucleic acids; Organic acids; RNA; Transcription; Tumors
Issue Date
2008-05
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.283, no.18, pp.11924 - 11934
Abstract
To understand the tumor-suppressing mechanism of the SWI/SNF chromatin remodeling complex, we investigated its molecular relationship with p53. Using the pREP4-luc episomal reporter, we first demonstrated that p53 utilizes the chromatin remodeling activity of the SWI/SNF complex to initiate transcription from the chromatin-structured promoter. Among the components of the SWI/SNF complex, we identified BAF60a as a mediator of the interaction with p53 by the yeast two-hybrid assay. p53 directly interacted only with BAF60a, but not with other components of the SWI/SNF complex, such as BRG1, SRG3, SNF5, or BAF57. We found out that multiple residues at the amino acid 108-150 region of BAF60a were involved in the interaction with the tetramerization domain of p53. The N-terminal fragment of BAF60a containing the p53-interacting region as well as small interfering RNA for baf60a inhibited the SWI/SNF complex-mediated transcriptional activity of p53. The uncoupling of p53 with the SWI/SNF complex resulted in the repression of both p53-dependent apoptosis and cell cycle arrest by the regulation of target genes. These results suggest that the SWI/SNF chromatin remodeling complex is involved in the suppression of tumors by the interaction with p53. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
URI
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DOI
10.1074/jbc.M705401200
ISSN
0021-9258
Appears in Collections:
PHY_Journal Papers
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