作者: Erik D. Holmstrom , Daniel Nettels , Benjamin Schuler
DOI: 10.1016/J.JMB.2017.10.010
关键词: Hepatitis C virus core 、 Genome 、 RNA 、 Crystallography 、 Core protein 、 Förster resonance energy transfer 、 Ribonucleoprotein 、 Biology 、 Hepatitis C virus 、 Biophysics
摘要: Many of the unanswered questions associated with hepatitis C virus assembly are related to core protein (HCVcp), which forms an oligomeric nucleocapsid encompassing viral genome. The structural properties HCVcp have been difficult quantify, at least in part because it is intrinsically disordered protein. We used single-molecule Forster Resonance Energy Transfer techniques study conformational dimensions and dynamics domain (HCVncd) various stages during RNA-induced formation nucleocapsid-like particles. Our results indicate that HCVncd a typical When small ribonucleoprotein complexes RNA hairpins from 3' end HCV genome, compacts but remains conformationally dynamic. Above critical concentration, these rapidly cooperatively assemble into large particles, wherein individual subunits become substantially more extended.