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Journal of Virology, December 1999, p. 9756-9763, Vol. 73, No. 12
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Activation Domain of Herpesvirus Saimiri R Protein Interacts with the TATA-Binding Protein

Kersten T. Hall, Alex J. Stevenson, Delyth J. Goodwin, Paul C. Gibson, Alex F. Markham, and Adrian Whitehouse*

Molecular Medicine Unit, University of Leeds, St. James's University Hospital, Leeds LS9 7TF, United Kingdom

Received 15 June 1999/Accepted 20 August 1999

The herpesvirus saimiri open reading frame (ORF) 50 produces two transcripts. The first is spliced, contains a single intron, and is detected at early times during the productive cycle, whereas the second is expressed later and is produced from a promoter within the second exon. Analysis of their gene products has shown that they function as sequence specific transactivators. In this report, we demonstrate that the carboxy terminus of ORF 50b contains an activation domain which is essential for transactivation. This domain contains positionally conserved hydrophobic residues found in a number of activation domains, including the herpes simplex virus VP16 and the Epstein-Barr virus R proteins. Mutational analysis of this domain demonstrates that these conserved hydrophobic residues are essential for ORF 50 transactivation capability. Furthermore, this domain is required for the interaction between the ORF 50 proteins and the basal transcription factor TATA-binding protein.

* Corresponding author. Mailing address: Molecular Medicine Unit, University of Leeds, St. James's University Hospital, Leeds LS9 7TF, United Kingdom. Phone: 44 (0)113 2066328. Fax: 44 (0)113 2444475. E-mail: a.whitehouse{at}leeds.ac.uk.

Journal of Virology, December 1999, p. 9756-9763, Vol. 73, No. 12
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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