Schumann, S, Baquero-Perez, B and Whitehouse, A orcid.org/0000-0003-3866-7110 (2016) Interactions between KSHV ORF57 and the novel human TREX proteins, CHTOP and CIP29. Journal of General Virology, 97. pp. 1904-1910. ISSN 0022-1317
Abstract
The coupling of mRNA processing steps is essential for precise and efficient gene expression. The human transcription/export (hTREX) complex is a highly conserved multi-protein complex responsible for eukaryotic mRNA stability and nuclear export. We have previously shown that the Kaposi's sarcoma-associated ORF57 protein orchestrates the recruitment of the hTREX complex onto viral intronless mRNA forming a stable and export competent viral ribonucleoprotein particle (vRNP). Recently, additional cellular proteins, namely CHTOP, CIP29 and POLDIP3 have been proposed as novel hTREX components. Herein we extend our previous research and provide evidence that ORF57 interacts with CHTOP and CIP29, in contrast to POLDIP3. Moreover, depletion studies show both CHTOP and CIP29 effect ORF57-mediated viral mRNA processing. As such, these results suggest both CHTOP and CIP29 are hTREX components and are recruited to an ORF57-mediated vRNP.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 The Authors. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) |
Funding Information: | Funder Grant number BBSRC BB/K000306/1 BBSRC BB/M006557/1 Cancer Research UK A19430 |
Depositing User: | Symplectic Publications |
Date Deposited: | 19 May 2016 10:23 |
Last Modified: | 11 Apr 2018 12:19 |
Published Version: | http://dx.doi.org/10.1099/jgv.0.000503 |
Status: | Published |
Publisher: | Microbiology Society |
Identification Number: | 10.1099/jgv.0.000503 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:99818 |