Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein.
Post-translational modifications of viral replication proteins could be widespread phenomena during the replication of plus-stranded RNA viruses. In this article, we identify two lysines in the tombusvirus p33 replication co-factor involved in ubiquitination and show that the same lysines are also important for the p33 to interact with the host Vps23p ESCRT-I factor. We find that the interaction of p33 with Vps23p is also affected by a "late-domain"-like sequence in p33. The combined mutations of the two lysines and the late-domain-like sequences in p33 reduced replication of a replicon RNA of Tomato bushy stunt virus in yeast model host, in plant protoplasts, and plant leaves, suggesting that p33-Vps23p ESCRT protein interaction affects tombusvirus replication. Using ubiquitin-mimicking p33 chimeras, we demonstrate that high level of p33 ubiquitination is inhibitory for TBSV replication. These findings argue that optimal level of p33 ubiquitination plays a regulatory role during tombusvirus infections.
Barajas
Daniel
D
Department of Plant Pathology, University of Kentucky, Lexington, KY 40546, USA.
Nagy
Peter D
PD
D056827:Endosomal Sorting Complexes Required for Transport / Q000378:metabolism*; D009154:Mutation; D018515:Plant Leaves / Q000821:virology; D010944:Plants / Q000821:virology; D011485:Protein Binding; D025941:Protein Interaction Mapping; D017864:Tombusvirus / Q000235:genetics / Q000502:physiology*; D054875:Ubiquitination; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D014779:Virus Replication; D015003:Yeasts / Q000821:virology
D056827:Endosomal Sorting Complexes Required for Transport; D014764:Viral Proteins