{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jiang X"],"funding":["National Natural Foundation of China"],"pagination":["1907"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9504981"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(9)"],"pubmed_abstract":["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 α-helix was recently found in the MET domain of RdRp. In this study, we further illustrate that the first α-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 α-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."],"journal":["Viruses"],"pubmed_title":["The N-Terminal α-Helix of Potato Virus X-Encoded RNA-Dependent RNA Polymerase Is Required for Membrane Association and Multimerization."],"pmcid":["PMC9504981"],"funding_grant_id":["32022071"],"pubmed_authors":["Luan Y","Chai M","Li Y","Yang Y","Jiang X","Wang Y","Deng W","Cheng X","Wu X"],"additional_accession":[]},"is_claimable":false,"name":"The N-Terminal α-Helix of Potato Virus X-Encoded RNA-Dependent RNA Polymerase Is Required for Membrane Association and Multimerization.","description":"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 α-helix was recently found in the MET domain of RdRp. In this study, we further illustrate that the first α-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 α-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.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2025-04-04T09:29:55.962Z","creation":"2025-04-04T09:29:55.962Z"},"accession":"S-EPMC9504981","cross_references":{"pubmed":["36146714"],"doi":["10.3390/v14091907"]}}