Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA

Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA

Nodamura virus (NoV) B2, a suppressor of RNA interference, binds double stranded RNAs (dsRNAs) and small interfering RNAs (siRNAs) corresponding to Dicer substrates and products. Here, we report that the amino terminal domain of NoV B2 (NoV B2 79) specifically binds siRNAs but not dsRNAs. NoV B2 79...

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Published in:Microbiology and Immunology
Main Author: Shaik Syed Ali P.; John J.; Selvaraj M.; Kek T.L.; Salleh M.Z.
Format: Article
Language:English
Published: 2015
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-84929724327&doi=10.1111%2f1348-0421.12253&partnerID=40&md5=10616efefea180c23bf33f705763b373
id 2-s2.0-84929724327
spelling 2-s2.0-84929724327
Shaik Syed Ali P.; John J.; Selvaraj M.; Kek T.L.; Salleh M.Z.
Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA
2015
Microbiology and Immunology
59
5
10.1111/1348-0421.12253
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84929724327&doi=10.1111%2f1348-0421.12253&partnerID=40&md5=10616efefea180c23bf33f705763b373
Nodamura virus (NoV) B2, a suppressor of RNA interference, binds double stranded RNAs (dsRNAs) and small interfering RNAs (siRNAs) corresponding to Dicer substrates and products. Here, we report that the amino terminal domain of NoV B2 (NoV B2 79) specifically binds siRNAs but not dsRNAs. NoV B2 79 oligomerizes on binding to 27 nucleotide siRNA. Mutation of the residues phenylalanine49 and alanine60 to cysteine and methionine, respectively enhances the RNA binding affinity of NoV B2 79. Circular dichroism spectra demonstrated that the wild type and mutant NoV B2 79 have similar secondary structure conformations. © 2015 The Societies and Wiley Publishing Asia Pty Ltd.

3855600
English
Article
All Open Access; Bronze Open Access
author Shaik Syed Ali P.; John J.; Selvaraj M.; Kek T.L.; Salleh M.Z.
spellingShingle Shaik Syed Ali P.; John J.; Selvaraj M.; Kek T.L.; Salleh M.Z.
Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA
author_facet Shaik Syed Ali P.; John J.; Selvaraj M.; Kek T.L.; Salleh M.Z.
author_sort Shaik Syed Ali P.; John J.; Selvaraj M.; Kek T.L.; Salleh M.Z.
title Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA
title_short Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA
title_full Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA
title_fullStr Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA
title_full_unstemmed Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA
title_sort Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA
publishDate 2015
container_title Microbiology and Immunology
container_volume 59
container_issue 5
doi_str_mv 10.1111/1348-0421.12253
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-84929724327&doi=10.1111%2f1348-0421.12253&partnerID=40&md5=10616efefea180c23bf33f705763b373
description Nodamura virus (NoV) B2, a suppressor of RNA interference, binds double stranded RNAs (dsRNAs) and small interfering RNAs (siRNAs) corresponding to Dicer substrates and products. Here, we report that the amino terminal domain of NoV B2 (NoV B2 79) specifically binds siRNAs but not dsRNAs. NoV B2 79 oligomerizes on binding to 27 nucleotide siRNA. Mutation of the residues phenylalanine49 and alanine60 to cysteine and methionine, respectively enhances the RNA binding affinity of NoV B2 79. Circular dichroism spectra demonstrated that the wild type and mutant NoV B2 79 have similar secondary structure conformations. © 2015 The Societies and Wiley Publishing Asia Pty Ltd.
publisher
issn 3855600
language English
format Article
accesstype All Open Access; Bronze Open Access
record_format scopus
collection Scopus
_version_ 1809677910568599552

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