Mono- and multi-ubiquitination alters the functions and subcellular localization of many cellular and viral proteins. Viruses can co-opt or actively manipulate the ubiquitin network to support viral processes or suppress innate immunity. Using yeast (. Saccharomyces cerevisiae) model host, we show that the yeast Rad6p (radiation sensitive 6) E2 ubiquitin-conjugating enzyme and its plant ortholog, AtUbc2, interact with two tombusviral replication proteins and these E2 ubiquitin-conjugating enzymes could be co-purified with the tombusvirus replicase. We demonstrate that TBSV RNA replication and the mono- and bi-ubiquitination level of p33 is decreased in rad6δ yeast. However, plasmid-based expression of AtUbc2p could complement both defects in rad6δ yeast. Knockdown of UBC2 expression in plants also decreases tombusvirus accumulation and reduces symptom severity, suggesting that Ubc2p is critical for virus replication in plants. We provide evidence that Rad6p is involved in promoting the subversion of Vps23p and Vps4p ESCRT proteins for viral replicase complex assembly.
|Number of pages||11|
|State||Published - Oct 1 2015|
Bibliographical noteFunding Information:
The authors thank to Dr. C. Boone (U. Toronto) for Cdc34 ts yeast. This work was supported by a grant for Overseas Researcher from Nihon University to Y. I. and by NSF ( MCB 1122039 ) to PDN.
© 2015 Elsevier Inc.
- Cell-free replication
- E2 ubiquitin-conjugating enzyme
- Host factor
- Virus replication
ASJC Scopus subject areas