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Title: Structural implications into dsRNA binding and RNA silencing suppression by NS3 protein of Rice Hoja Blanca Tenuivirus
Authors: Yang, X.
Tan, S.H.
Teh, Y.J.
Yuan, Y.A. 
Keywords: Crystal structure
DsRNA binding
Rice Hoja Blanca Tenuivirus NS3
RNA silencing suppression
Issue Date: May-2011
Citation: Yang, X., Tan, S.H., Teh, Y.J., Yuan, Y.A. (2011-05). Structural implications into dsRNA binding and RNA silencing suppression by NS3 protein of Rice Hoja Blanca Tenuivirus. RNA 17 (5) : 903-911. ScholarBank@NUS Repository.
Abstract: Rice Hoja Blanca Tenuivirus (RHBV), a negative strand RNA virus, has been identified to infect rice and is widely transmitted by the insect vector. NS3 protein encoded by RHBV RNA3 was reported to be a potent RNAi suppressor to counterdefense RNA silencing in plants, insect cells, and mammalian cells. Here, we report the crystal structure of the N-terminal domain of RHBV NS3 (residues 21-114) at 2.0 Å RHBV NS3 N-terminal domain forms a dimer by two pairs of α-helices in an anti-parallel mode, with one surface harboring a shallow groove at the dimension of 20 Å 3 30 Å for putative dsRNA binding. In vitro RNA binding assay and RNA silencing suppression assay have demonstrated that the structural conserved residues located along this shallow groove, such as Arg50, His51, Lys77, and His85, participate in dsRNA binding and RNA silencing suppression. Our results provide the initial structural implications in understanding the RNAi suppression mechanism by RHBV NS3. Copyright © 2011 RNA Society.
Source Title: RNA
ISSN: 13558382
DOI: 10.1261/rna.2552811
Appears in Collections:Staff Publications

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