| pubmed-article:11304541 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11304541 | lifeskim:mentions | umls-concept:C0087111 | lld:lifeskim |
| pubmed-article:11304541 | lifeskim:mentions | umls-concept:C1333336 | lld:lifeskim |
| pubmed-article:11304541 | lifeskim:mentions | umls-concept:C0600531 | lld:lifeskim |
| pubmed-article:11304541 | lifeskim:mentions | umls-concept:C0063701 | lld:lifeskim |
| pubmed-article:11304541 | lifeskim:mentions | umls-concept:C0031586 | lld:lifeskim |
| pubmed-article:11304541 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:11304541 | pubmed:dateCreated | 2001-6-11 | lld:pubmed |
| pubmed-article:11304541 | pubmed:abstractText | Interferon regulatory factor-2 (IRF-2) is a transcription factor of the IRF family that represses interferon-mediated gene expression. In the present study, we show that human monocytic U937 cells express truncated forms of IRF-2 containing the DNA binding domain but lacking much of the C-terminal regulatory domain. U937 cells are shown to respond to phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) to induce expression of histone acetylases p300 and p300/CBP-associated factor (PCAF). In addition, TPA treatment led to the appearance of full-length IRF-2, along with a reduction of the truncated protein. Interestingly, full-length IRF-2 in TPA-treated U937 cells occurred as a complex with p300 as well as PCAF and was itself acetylated. Consistent with these results, recombinant IRF-2 was acetylated by p300 and to a lesser degree by PCAF in vitro. Another IRF member, IRF-1, an activator of interferon-mediated transcription, was also acetylated in vitro by these acetylases. Finally, we demonstrate that the addition of IRF-2 but not IRF-1 inhibits core histone acetylation by p300 in vitro. The addition of IRF-2 also inhibited acetylation of nucleosomal histones in TPA-treated U937 cells. Acetylated IRF-2 may affect local chromatin structure in vivo by inhibiting core histone acetylation and may serve as a mechanism by which IRF-2 negatively regulates interferon-inducible transcription. | lld:pubmed |
| pubmed-article:11304541 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11304541 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11304541 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11304541 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11304541 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11304541 | pubmed:author | pubmed-author:OzatoKK | lld:pubmed |
| pubmed-article:11304541 | pubmed:author | pubmed-author:MasumiAA | lld:pubmed |
| pubmed-article:11304541 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11304541 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11304541 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11304541 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11304541 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11304541 | pubmed:pagination | 20973-80 | lld:pubmed |
| pubmed-article:11304541 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11304541 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11304541 | pubmed:articleTitle | Coactivator p300 acetylates the interferon regulatory factor-2 in U937 cells following phorbol ester treatment. | lld:pubmed |
| pubmed-article:11304541 | pubmed:affiliation | Department of Safety Research on Biologics, National Institute of Infectious Diseases, Tokyo 208-0011, Japan. | lld:pubmed |
| pubmed-article:11304541 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11304541 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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