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Nucleic Acids Research 2004 32(12):3632-3641; doi:10.1093/nar/gkh692
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Published online 8 July 2004

Nucleic Acids Research, Vol. 32 No. 12 © Oxford University Press 2004; all rights reserved

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

Chandrani Chattopadhyay1, David Hawke2, Ryuji Kobayashi2 and Sankar N. Maity1,3,*

1 Department of Molecular Genetics and 2 Department of Molecular Pathology, M.D. Anderson Cancer Center and 3 Genes and Development Program, Graduate School of Biomedical Sciences, The University of Texas, Houston, TX 77030, USA

* To whom correspondence should be addressed. Tel: +1 713 792 8943; Fax: +1 713 794 4295; Email: smaity{at}mdanderson.org

Received April 23, 2004; Revised and Accepted June 18, 2004

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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