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RNA binding property and RNA chaperone activity of dengue virus core protein and other viral RNA‐interacting proteins
Author(s) -
Pong Wen-Li,
Huang Zhi-Shun,
Teoh Pak-Guan,
Wang Chung-Chun,
Wu Huey-Nan
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.06.038
Subject(s) - rna , rna dependent rna polymerase , ns3 , ribozyme , dengue virus , non coding rna , virology , dengue fever , rna helicase a , biology , hammerhead ribozyme , chemistry , microbiology and biotechnology , helicase , biochemistry , virus , gene , hepatitis c virus
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.