International Immunology, Vol. 15, No. 4, pp. 467-475,
April 2003
© 2003 Japanese Society for Immunology
MHC class II enhanceosome: how is the class II transactivator recruited to DNA-bound activators?
1 Department of Surgery and Comprehensive Cancer Center, and 2 Rosalind Russell Medical Research Center, and Departments of Medicine, Microbiology and Immunology, University of California San Francisco, CA 94115-0703, USA 3 Institute of Biochemistry, Medical Faculty, University of Ljubljana, Vrazov trg 2, 1000 Ljubljana, Republic of Slovenia 4 Department of Clinical and Biological Sciences, University of Insubria, Varese, Italy
Correspondence to: B. M. Peterlin, N215, UCSF Mt Zion Cancer Center, 2340 Sutter Street, San Francisco, CA 94115-0703, USA. E-mail: matija{at}itsa.ucsf.edu
Transmitting editor: L. Steinman
MHC class II (MHCII) determinants play a crucial role in the immune response by presenting antigenic peptides to T cells. Their expression is controlled from compact promoters at the transcriptional level. Pre-assembled regulatory factor X (RFX) and nuclear factor Y (NFY) complexes form a platform on DNA. The class II transactivator (CIITA) can then be recruited through multiple protein–protein interactions. In this report, we defined domains of CIITA that are responsible for its interactions with these DNA-bound factors. Furthermore, using DNA-affinity precipitation, we demonstrated that although CIITA binds at least five activators, RFX5, RFXAP, RFXANK/B, NFYB and NFYC, its assembly on the promoter requires the addition of nuclear extracts. We conclude that not only does the platform bind DNA via multiple, spatially constrained nteractions, but that it can recruit only modified and/or complexed CIITA to MHCII promoters.
Keywords: activator, assembly, nuclear factor Y, regulatory factor X, transcription
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