Nucleic Acids Research Advance Access originally published online on August 12, 2006
Nucleic Acids Research 2006 34(14):3938-3946; doi:10.1093/nar/gkl539
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Nucleic Acids Research, 2006, Vol. 34, No. 14 3938-3946
© 2006 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Nucleic Acid Enzymes |
Characterization of RNA helicase A as component of STAT6-dependent enhanceosome
1 Institute of Medical Technology, University of Tampere FI-33014 Tampere, Finland 2 Department of Immunology, Tianjin Medical University Tianjin 300070, Peoples Republic of China 3 Department of Clinical Microbiology, Tampere University Hospital FI-33521 Tampere, Finland
*To whom correspondence should be addressed. Tel: +358 3 3551 7845; Fax: +358 3 3551 8597; Email: olli.silvennoinen{at}uta.fi
Received April 9, 2006. Revised July 8, 2006. Accepted July 13, 2006.
Signal transducer and activator of transcription 6 (STAT6) is a regulator of transcription for interleukin-4 (IL-4)-induced genes. The ability of STAT6 to activate transcription depends on functional interaction with other transcription factors and coactivators. We have characterized the mechanism of STAT6-mediated transcriptional activation by identifying STAT6 transcription activation domain (TAD) interacting nuclear proteins. The first of the identified proteins was coactivator protein p100, which regulates IL-4-induced transcription by connecting STAT6 with other transcriptional regulators. Here, we describe RNA helicase A (RHA) as a novel component of STAT6 transcriptosome. In vitro and in vivo experiments indicated that RHA did not directly interact with STAT6, but p100 protein was found to mediate the assembly of the ternary complex of STAT6-p100-RHA. In chromatin immunoprecipitation studies RHA together with p100 enhanced the binding of STAT6 on the human Ig
promoter after IL-4 stimulation. RHA enhanced the IL-4-induced transcription, and the participation of RHA in IL-4-regulated transcription was supported by RNAi experiments. Our results suggest that RHA has an important role in the assembly of STAT6 transcriptosome. As RHA is also known to interact with chromatin modifying proteins, the RHA containing protein complexes may facilitate the entry of transcriptional apparatus to the IL-4 responsive promoters.
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