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Backbone and sidechain methyl Ile (δ1), Leu and Val chemical shift assignments of RDE-4 (1–243), an RNA interference initiation protein in C. elegans

Backbone and sidechain methyl Ile (δ1), Leu and Val chemical shift assignments of RDE-4 (1–243),... The RNAi pathway of several organisms requires presence of double stranded RNA binding proteins for functioning of Dicer in gene regulation. In C. elegans, a double stranded RNA binding protein, RDE-4 (385 aa, 44 kDa) recognizes long exogenous dsRNA and initiates the RNAi pathway. We have achieved complete backbone and stereospecific methyl sidechain Ile (δ1), Leu and Val chemical shifts of first 243 amino acids of RDE-4, namely RDE-4ΔC. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

Backbone and sidechain methyl Ile (δ1), Leu and Val chemical shift assignments of RDE-4 (1–243), an RNA interference initiation protein in C. elegans

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References (13)

Publisher
Springer Journals
Copyright
Copyright © 2011 by Springer Science+Business Media B.V.
Subject
Physics; Biophysics and Biological Physics; Biochemistry, general; Polymer Sciences
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-011-9343-0
pmid
22002349
Publisher site
See Article on Publisher Site

Abstract

The RNAi pathway of several organisms requires presence of double stranded RNA binding proteins for functioning of Dicer in gene regulation. In C. elegans, a double stranded RNA binding protein, RDE-4 (385 aa, 44 kDa) recognizes long exogenous dsRNA and initiates the RNAi pathway. We have achieved complete backbone and stereospecific methyl sidechain Ile (δ1), Leu and Val chemical shifts of first 243 amino acids of RDE-4, namely RDE-4ΔC.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Oct 15, 2011

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