Xue Jiang
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Xue Jiang has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
- Mengzhu Chai
College of Agriculture, Northeast Agricultural University, Harbin 150030, China
1 shared publication - Wenjia Deng
College of Agriculture, Northeast Agricultural University, Harbin 150030, China
1 shared publication - Xiaofei Cheng
College of Plant Protection Northeast Agricultural University Harbin Heilongjiang China
1 shared publication - Xiaoyun Wu
College of Plant Protection, Northeast Agricultural University, Harbin, Heilongjiang, P. R. China.
1 shared publication - Yameng Luan
College of Agriculture, Northeast Agricultural University, Harbin 150030, China
1 shared publication - Yingshuai Yang
College of Agriculture, Northeast Agricultural University, Harbin 150030, China
1 shared publication
Latest Publications
- Open Access
The N-Terminal α-Helix of Potato Virus X-Encoded RNA-Dependent RNA Polymerase Is Required for Membrane Association and Multimerization
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.
Open AccessThe N-Terminal α-Helix of Potato Virus X-Encoded RNA-Dependent RNA Polymerase Is Required for Membrane Association and Multimerization
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.