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Chemical shift assignments of DRB4 (1–153), a dsRNA binding protein in A. thaliana RNAi pathway

Chemical shift assignments of DRB4 (1–153), a dsRNA binding protein in A. thaliana RNAi pathway RNA interference (RNAi) is a conserved biological response to dsRNA and regulates the expression of protein-coding genes to mediate resistance to both endogenous parasitic and exogenous pathogenic nucleic acids. In RNAi pathway, dsRNA binding proteins assists Dicer at various stages of RNAi. In plants, DRB4, is a multidomain protein containing two dsRNA binding domains that recognizes the long exogenous/endogenous dsRNA and presents it to Ribonuclease enzyme, Dicer like 4, resulting in the production of 21 nt small interfering RNA. Here, we report nearly complete backbone and sidechain chemical shift assignments of N-terminus of DRB4 (1–153, ~18 kDa), containing both double stranded RNA binding domains and the linker. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

Chemical shift assignments of DRB4 (1–153), a dsRNA binding protein in A. thaliana RNAi pathway

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References (25)

Publisher
Springer Journals
Copyright
Copyright © 2014 by Springer Science+Business Media Dordrecht
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-014-9585-8
pmid
25281003
Publisher site
See Article on Publisher Site

Abstract

RNA interference (RNAi) is a conserved biological response to dsRNA and regulates the expression of protein-coding genes to mediate resistance to both endogenous parasitic and exogenous pathogenic nucleic acids. In RNAi pathway, dsRNA binding proteins assists Dicer at various stages of RNAi. In plants, DRB4, is a multidomain protein containing two dsRNA binding domains that recognizes the long exogenous/endogenous dsRNA and presents it to Ribonuclease enzyme, Dicer like 4, resulting in the production of 21 nt small interfering RNA. Here, we report nearly complete backbone and sidechain chemical shift assignments of N-terminus of DRB4 (1–153, ~18 kDa), containing both double stranded RNA binding domains and the linker.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Oct 4, 2014

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