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

Kevin J. Colgan, James R. Boyne, Andrian Whitehouse

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Herpesvirus saimiri (HVS) ORF57 nucleocytoplasmic shuttle protein binds viral RNA and interacts with the cellular nuclear export adaptor protein, Aly, to access the TAP-mediated nuclear export pathway. This enables the efficient nuclear export of HVS intronless mRNAs. Herein, we extend these studies and demonstrate that ORF57 recruits several members of hTREX, namely Aly, UAP56 and hTHO-complex proteins, onto the viral mRNAs to assemble 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 mRNA nuclear export and replication.

Original languageEnglish
Pages (from-to)1455-1460
Number of pages6
JournalJournal of General Virology
Volume90
Issue number6
Early online date1 Jun 2009
DOIs
Publication statusPublished - 3 Aug 2009
Externally publishedYes

Fingerprint Dive into the research topics of 'Uncoupling of hTREX demonstrates that UAP56 and hTHO-complex recruitment onto herpesvirus saimiri intronless transcripts is required for replication'. Together they form a unique fingerprint.

Cite this