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Structural basis for dimerization of a paramyxovirus polymerase complex

Nature Communications. 2024-04; 
Jin Xie, Mohamed Ouizougun-Oubari, Li Wang, Guanglei Zhai, Daitze Wu, Zhaohu Lin, Manfu Wang, Barbara Ludeke, Xiaodong Yan, Tobias Nilsson, Lu Gao, Xinyi Huang, Rachel Fearns, Shuai Chen
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Proteins, Expression, Isolation and Analysis After high-speed centrifugation at 50,000× g for 60?min at 4?°C, the supernatant containing the target proteins was loaded onto anti-FLAG G1 affinity resin (Genscript).? Get A Quote

摘要

The transcription and replication processes of non-segmented, negative-strand RNA viruses (nsNSVs) are catalyzed by a multi-functional polymerase complex composed of the large protein (L) and a cofactor protein, such as phosphoprotein (P). Previous studies have shown that the nsNSV polymerase can adopt a dimeric form, however, the structure of the dimer and its function are poorly understood. Here we determine a 2.7 ? cryo-EM structure of human parainfluenza virus type 3 (hPIV3) L-P complex with the connector domain (CD') of a second L built, while reconstruction of the rest of the second L-P obtains a low-resolution map of the ring-like L core region. This study reveals detailed atomic features of nsNSV polym... More

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