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. 1993 Oct;13(10):6375–6384. doi: 10.1128/mcb.13.10.6375

RFX1 is identical to enhancer factor C and functions as a transactivator of the hepatitis B virus enhancer.

C A Siegrist 1, B Durand 1, P Emery 1, E David 1, P Hearing 1, B Mach 1, W Reith 1
PMCID: PMC364696  PMID: 8413236

Abstract

Hepatitis B virus gene expression is to a large extent under the control of enhancer I (EnhI). The activity of EnhI is strictly dependent on the enhancer factor C (EF-C) site, an inverted repeat that is bound by a ubiquitous nuclear protein known as EF-C. Here we report the unexpected finding that EF-C is in fact identical to RFX1, a novel transcription factor previously cloned by virtue of its affinity for the HLA class II X-box promoter element. This finding has allowed us to provide direct evidence that RFX1 (EF-C) is crucial for EnhI function in HepG2 hepatoma cells; RFX1-specific antisense oligonucleotides appear to inhibit EnhI-driven expression of the hepatitis B virus major surface antigen gene, and in transfection assays, RFX1 behaves as a potent transactivator of EnhI. Interestingly, transactivation of EnhI by RFX1 (EF-C) is not observed in cell lines that are not of liver origin, suggesting that the ubiquitous RFX1 protein cooperates with liver-specific factors.

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Selected References

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