期刊
NUCLEIC ACIDS RESEARCH
卷 32, 期 12, 页码 3632-3641出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkh692
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资金
- NCI NIH HHS [P30 CA016672, CA16672] Funding Source: Medline
- NIAMS NIH HHS [AR46264, R01 AR046264] Funding Source: Medline
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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