RNA binding property and RNA chaperone activity of dengue virus core protein and other viral RNA-interacting proteins

• Published in: FEBS letters 2011-08, Vol.585 (16), p.2575-2581
• Main Authors: Pong, Wen-Li, Huang, Zhi-Shun, Teoh, Pak-Guan, Wang, Chung-Chun, Wu, Huey-Nan
• Format: Article
• Language: English
• Subjects: Base Sequence; Core protein; Dengue Virus; DENV; Genome, Viral - genetics; Molecular Chaperones - metabolism; NS3 helicase; NS5; Nucleic Acid Conformation; Protein Binding; Protein Engineering; RNA binding protein; RNA chaperone; RNA Helicases - metabolism; RNA, Catalytic - genetics; RNA, Viral - chemistry; RNA, Viral - genetics; RNA, Viral - metabolism; Serine Endopeptidases - metabolism; Strand annealing; Viral Core Proteins - metabolism; Viral Nonstructural Proteins - metabolism
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2011.06.038

► DENV-3 core protein forms an α-helix-rich dimer, binds RNA and facilitates the strand annealing process. ► DENV core protein facilitates hammerhead structure formation by acting as an RNA chaperone. ► DENV NS5 has a weak RNA chaperone activity. ► DENV NS3 helicase failed to refold RNA with a complex secondary structure. In this study we showed that the dengue virus (DENV) core protein forms a dimer with an α-helix-rich structure, binds RNA and facilitates the strand annealing process. To assess the RNA chaperone activity of this core protein and other dengue viral RNA-interacting proteins, such as NS3 helicase and NS5 proteins, we engineered cis- and trans-cleavage hammerhead ribozyme constructs carrying DENV genomic RNA elements. Our results indicate that DENV core protein facilitates typical hammerhead structure formation by acting as an RNA chaperone and DENV NS5 has a weak RNA chaperone activity, while DENV NS3 helicase failed to refold RNA with a complex secondary structure.