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

被引：44

作者：

Pong, Wen-Li ^{[1
]}

Huang, Zhi-Shun ^{[1
]}

Teoh, Pak-Guan ^{[1
,2
]}

Wang, Chung-Chun ^{[1
]}

Wu, Huey-Nan ^{[1
]}

机构：

[1] Acad Sinica, Inst Mol Biol, Taipei, Taiwan

[2] Natl Def Med Ctr, Grad Inst Life Sci, Taiwan Int Grad Program, Taipei, Taiwan

来源：

FEBS LETTERS | 2011年 / 585卷 / 16期

关键词：

DENV; Core protein; NS5; NS3; helicase; RNA chaperone; Strand annealing; RNA binding protein; REPLICATION;

D O I：

10.1016/j.febslet.2011.06.038

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2575 / 2581

页数：7

共 24 条

[1] De novo synthesis of RNA by the dengue virus RNA-dependent RNA polymerase exhibits temperature dependence at the initiation but not elongation phase [J].