Human p32, interacts with B subunit of the CCAAT-binding factor, CBF/NF-Y, and inhibits CBF-mediated transcription activation in vitro

Nucleic Acids Research
Chandrani ChattopadhyaySankar N Maity

Abstract

To understand the role of the CCAAT-binding factor, CBF, in transcription, we developed a strategy to purify the heterotrimeric CBF complex from HeLa cell extracts using two successive immunoaffinity chromatography steps. Here we show that the p32 protein, previously identified as the ASF/SF2 splicing factor-associated protein, copurified with the CBF complex. Studies of protein-protein interaction demonstrated that p32 interacts specifically with CBF-B subunit and also associates with CBF-DNA complex. Cellular localization by immunofluorescence staining revealed that p32 is present in the cell throughout the cytosol and nucleus, whereas CBF is present primarily in the nucleus. A portion of the p32 colocalizes with CBF-B in the nucleus. Interestingly, reconstitution of p32 in an in vitro transcription reaction demonstrated that p32 specifically inhibits CBF-mediated transcription activation. Altogether, our study identified p32 as a novel and specific corepressor of CBF-mediated transcription activation in vitro.

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Citations

Jan 4, 2008·Human Genetics·Beatriz Aranda-OrgillésSusann Schweiger
Mar 18, 2006·Apoptosis : an International Journal on Programmed Cell Death·Anupama Kamal, K Datta
Jan 19, 2007·Journal of Virology·Jennifer A MertzJaquelin P Dudley
Nov 5, 2011·Critical Reviews in Biochemistry and Molecular Biology·Diletta DolfiniRoberto Mantovani
Jun 26, 2015·Molecular Biology of the Cell·Gabrielle A Roloff, Michael F Henry
Apr 16, 2010·The Journal of Biological Chemistry·Mareen SpreheMaria A Schumacher
Sep 22, 2006·Human Molecular Genetics·Claire L NavarroNicolas Lévy
Mar 7, 2021·International Journal of Molecular Sciences·Hongni XueZekun Guo

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