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Journal of Virology, October 2006, p. 10274-10280, Vol. 80, No. 20
0022-538X/06/$08.00+0     doi:10.1128/JVI.00995-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Human Cytomegalovirus UL84 Protein Contains Two Nuclear Export Signals and Shuttles between the Nucleus and the Cytoplasm

Peter Lischka, Claudia Rauh, Regina Mueller, and Thomas Stamminger*

Institut für Klinische und Molekulare Virologie der Universität Erlangen-Nürnberg, D-91054 Erlangen, Germany

Received 15 May 2006/ Accepted 20 July 2006

Previous studies defined pUL84 of human cytomegalovirus as an essential regulatory protein with nuclear localization that was proposed to act during initiation of viral-DNA synthesis. Recently, we demonstrated that a complex domain of 282 amino acids within pUL84 functions as a nonconventional nuclear localization signal. Sequence inspection of this domain revealed the presence of motifs with homology to leucine-rich nuclear export signals. Here, we report the identification of two functional, autonomous nuclear export signals and show that pUL84 acts as a CRM-1-dependent nucleocytoplasmic shuttling protein. This suggests an unexpected cytoplasmic role for this essential viral regulatory protein.

* Corresponding author. Mailing address: Institut für Klinische und Molekulare Virologie, Universität Erlangen-Nürnberg, Schlossgarten 4, D-91054 Erlangen, Germany. Phone: 49 9131 8526783. Fax: 49 9131 8522101. E-mail: tsstammi{at}viro.med.uni-erlangen.de.

Journal of Virology, October 2006, p. 10274-10280, Vol. 80, No. 20
0022-538X/06/$08.00+0     doi:10.1128/JVI.00995-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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