Journal
JOURNAL OF GENERAL VIROLOGY
Volume 90, Issue -, Pages 1455-1460Publisher
MICROBIOLOGY SOC
DOI: 10.1099/vir.0.010124-0
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Funding
- BBSRC DTG
- BBSRC [BBSB03475, BB/F012101/1]
- Leverhulme Trust fellowship
- Biotechnology and Biological Sciences Research Council [BB/F012101/1] Funding Source: researchfish
- BBSRC [BB/F012101/1] Funding Source: UKRI
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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.
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