Journal
VIRUSES-BASEL
Volume 14, Issue 9, Pages -Publisher
MDPI
DOI: 10.3390/v14091907
Keywords
potato virus X; membrane association; methyltransferase; multimerization; RNA-dependent RNA polymerase
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Funding
- National Natural Foundation of China [32022071]
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This study reveals the association mechanism and multimerization process of RNA-dependent RNA polymerase with endoplasmic reticulum during the replication of potato virus X.
Positive-sense single-stranded RNA viruses replicate in virus-induced membranous organelles for maximum efficiency and immune escaping. The replication of potato virus X (PVX) takes place on the endoplasmic reticulum (ER); however, how PVX-encoded RNA-dependent RNA polymerase (RdRp) is associated with the ER is still unknown. A proline-kinked amphipathic alpha-helix was recently found in the MET domain of RdRp. In this study, we further illustrate that the first alpha-helix of the MET domain is also required for ER association. Moreover, we found that the MET domain forms multimers on ER and the first alpha-helix is essential for multimerization. These results suggest that the RdRp of PVX adopts more than one hydrophobic motif for membrane association and for multimerization.
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