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

Biomol NMR Assign. 2012 Oct;6(2):143-6. doi: 10.1007/s12104-011-9343-0. Epub 2011 Oct 15.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry*
  • Animals
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins / chemistry*
  • Isoleucine / chemistry
  • Leucine / chemistry
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • RNA Interference*
  • RNA-Binding Proteins / chemistry*
  • Valine / chemistry

Substances

  • Amino Acids
  • Caenorhabditis elegans Proteins
  • RDE-4 protein, C elegans
  • RNA-Binding Proteins
  • Isoleucine
  • Leucine
  • Valine