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Journal of Virology, June 2009, p. 6300-6305, Vol. 83, No. 12
0022-538X/09/$08.00+0     doi:10.1128/JVI.00054-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Analysis of the Varicella-Zoster Virus IE62 N-Terminal Acidic Transactivating Domain and Its Interaction with the Human Mediator Complex{triangledown}

Shinobu Yamamoto,1 Alexander Eletsky,2,3 Thomas Szyperski,2,3 John Hay,1 and William T. Ruyechan1*

Departments of Microbiology and Immunology,1 Chemistry, University at Buffalo SUNY, Buffalo, New York 14214,2 Northeast Structural Genomics Consortium, Rutgers University, Piscataway, New Jersey3

Received 9 January 2009/ Accepted 2 April 2009

The varicella-zoster virus major transactivator, IE62, contains a potent N-terminal acidic transcriptional activation domain (TAD). Our experiments revealed that the minimal IE62 TAD encompasses amino acids (aa) 19 to 67. We showed that the minimal TAD interacts with the human Mediator complex. Site-specific mutations revealed residues throughout the minimal TAD that are important for both activation and Mediator interaction. The TAD interacts directly with aa 402 to 590 of the MED25 subunit, and site-specific TAD mutations abolished this interaction. Two-dimensional nuclear magnetic resonance spectroscopy revealed that the TAD is intrinsically unstructured. Our studies suggest that transactivation may involve the TAD adopting a defined structure upon binding MED25.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, 138 Farber Hall, 3435 Main St., University at Buffalo, SUNY, Buffalo, NY 14214. Phone: (716) 829-2312. Fax: (716) 829-2376. E-mail: ruyechan{at}buffalo.edu

{triangledown} Published ahead of print on 8 April 2009.

Journal of Virology, June 2009, p. 6300-6305, Vol. 83, No. 12
0022-538X/09/$08.00+0     doi:10.1128/JVI.00054-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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