Highly Acidic C-Terminal Domain of pp32 Is Required for the Interaction with Histone Chaperone, TAF-Ibeta(Molecular and Cell Biology)
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概要
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We have previously reported that INHAT (inhibitor of acetyltransferases) complex subunits, TAF (template activating factor)-Ialpha, TAF-Ibeta and pp32 can inhibit histone acetylation and HAT (histone acetyltransferase)-dependent transcription by binding to histones. Evidences are accumulating that INHAT complex subunits have important regulatory roles in various cellular activities such as replication, transcription, and apoptosis etc. However, how these subunits interact each other remains largely unknown. Using immunoprecipitation (IP) and protein-protein interaction assays with TAF-Ibeta and pp32 deletion mutant proteins, we identify INHAT complex subunits, TAF-Ibeta and pp32 interaction requires highly acidic C-terminal domain of pp32. We also show that the interaction between the INHAT complex subunits is stronger in the presence of histones. In this study, we report that the synergistic inhibition of HAT-mediated transcription by TAF-Ibeta and pp32 is dependent on the highly acidic C-terminal domain of pp32.
- 2006-12-01
著者
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SEO Sang-Beom
Department of Life Science, College of Natural Sciences, Chung-Ang University
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Seo Sang-beom
Department Of Life Science College Of Natural Sciences Chung-ang University
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LEE In-Seon
Department of Materials Engineering, Korea University of Technology and Education
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Oh Sang-min
Department Of Life Science College Of Natural Sciences Chung-ang University
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Lee In-seon
Department Of Life Science College Of Natural Sciences Chung-ang University
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Lee Dong-seok
Division Of Animal Biotechnology College Of Animal Resources Science Kangwon National University
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KIM Sung-Mi
Department of Life Science, College of Natural Sciences, Chung-Ang University
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Kim Sung-mi
Department Of Life Science College Of Natural Sciences Chung-ang University
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Lee In-seon
Department Of Food Science And Technology Keimyung University
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