Journal
FEBS LETTERS
Volume 585, Issue 16, Pages 2575-2581Publisher
WILEY
DOI: 10.1016/j.febslet.2011.06.038
Keywords
DENV; Core protein; NS5; NS3 helicase; RNA chaperone; Strand annealing; RNA binding protein
Funding
- National Science Council [NSC-98-2320-B-001-013-MY3]
- National Health Research Institute [NHRI-EX99-9745SI]
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In this study we showed that the dengue virus (DENV) core protein forms a dimer with an alpha-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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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