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Papers In Press, published online ahead of print July 25, 2001
Oncology Center, The Johns Hopkins University, Baltimore, MD 21231-1001
Corresponding Author: parowe{at}jhmi.edu
Summary: Type I interferon plays a critical role in the innate immunity against viral infection. Expression of IFNA genes in infected cells is cell type-dependent and is regulated at the transcriptional level. Present study is focused on the molecular mechanism underlying the differential expression of human IFNA1 and A2 genes. Two nucleotides, at position, -98 and -81 of IFNA1 and A2 promoter, were pivotal to the differential expression. The DNA pull-down and chromatin precipitation assays have shown that nuclear IRF-3 and IRF-7 as well as IRF-1 bind to IFNA1 VRE. Interestingly, overexpression of IRF-7 increased the otherwise weak binding of both IRF-3 and IRF-7 to IFNA2 VRE. This data together with the results of two-step chromatin imunoprecipitation strongly suggest that the IRF-3 and IRF-7 bind to IFNA1 promoter as a dimer. Furthermore binding of IRF-3 and IRF-7 to IFNA VRE is associated with the presence of acetylated histone H3, suggesting that histone acetyl transferase(s) is tethered together with virus-activated IRF-3 and IRF-7 to the IFNA1 promoter. In addition, the constitutively active IRF-3 and IRF-7 mutants activate the endogenous IFNA genes in uninfected cells, however the expression profile of IFNA is not identical to that induced by viral infection.
J. Biol. Chem, 10.1074/jbc.M105121200
Submitted on June 4, 2001
Revised on July 25, 2001
Accepted on July 24, 2001
Recruitment of multiple interferon regulatory factors and histone acetyl transferase to the transcriptionally active IFNA promoters
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