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Uncoupling of hTREX demonstrates that UAP56 and hTHO-complex recruitment onto herpesvirus saimiri intronless transcripts is required for replication

University of Leeds

¹ E-mail: a.whitehouse{at}leeds.ac.uk

Herpesvirus saimiri (HVS) ORF57 nucleo-cytoplasmic shuttle protein binds viral RNA and interacts with the cellular nuclear export adapter protein, Aly, to access the TAP-mediated nuclear export pathway. These properties enable the efficient nuclear export of HVS intronless mRNAs. Herein, we extend these studies and demonstrate that ORF57 recruits all core members of hTREX, namely Aly, UAP56 and hTHO-complex proteins onto the viral mRNA to assembly an export competent ribonucleoprotein particle. Moreover, using a transdominant form of Aly which inhibits UAP56 and hTHO-complex association with viral intronless mRNA, we show that complete hTREX recruitment is required for efficient HVS replication.

Received 6 January 2009; accepted 23 February 2009.