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Molecular and Cellular Biology, April 1999, p. 2791-2802, Vol. 19, No. 4
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

A Kinase Activity Associated with Simian Virus 40 Large T Antigen Phosphorylates Upstream Binding Factor (UBF) and Promotes Formation of a Stable Initiation Complex between UBF and SL1

Weiguo Zhai and Lucio Comai*

Department of Molecular Microbiology and Immunology and Norris Comprehensive Cancer Center, University of Southern California School of Medicine, Los Angeles, California 90033

Received 24 August 1998/Returned for modification 1 October 1998/Accepted 14 January 1999

Simian virus 40 large T antigen is a multifunctional protein which has been shown to modulate the expression of genes transcribed by RNA polymerase I (Pol I), II, and III. In all three transcription systems, a key step in the activation process is the recruitment of large T antigen to the promoter by direct protein-protein interaction with the TATA binding protein (TBP)-TAF complexes, namely, SL1, TFIID, and TFIIIB. However, our previous studies on large T antigen stimulation of Pol I transcription also revealed that the binding to the TBP-TAFI complex SL1 is not sufficient to activate transcription. To further define the molecular mechanism involved in large T antigen-mediated Pol I activation, we examined whether the high-mobility group box-containing upstream binding factor (UBF) plays any role in this process. Here, using cell labeling experiments, we showed that large T antigen expression induces an increase in UBF phosphorylation. Further biochemical analysis demonstrated that UBF is phosphorylated by a kinase activity that is strongly associated with large T antigen, and that the carboxy-terminal activation domain of UBF is required for the phosphorylation to occur. Using in vitro reconstituted transcription assays, we demonstrated that the inability of alkaline phosphatase treated UBF to efficiently activate transcription can be rescued by large T antigen. Moreover, we showed that large T antigen-induced UBF phosphorylation promotes the formation of a stable UBF-SL1 complex. Together, these results provide strong evidence for an important role for the large T antigen-associated kinase in mediating the stimulation of RNA Pol I transcription.

* Corresponding author. Mailing address: Department of Molecular Microbiology and Immunology and Norris Comprehensive Cancer Center, University of Southern California School of Medicine, 2011 Zonal Ave., HMR 509, Los Angeles, CA 90033. Phone: (323) 442-3950. Fax: (323) 442-1721. E-mail: comai{at}hsc.usc.edu.

Molecular and Cellular Biology, April 1999, p. 2791-2802, Vol. 19, No. 4
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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