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

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...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2012-10, Vol.6 (2), p.143-146
Main Authors: Chiliveri, Sai Chaitanya, Kumar, Sonu, Marelli, Udaya Kiran, Deshmukh, Mandar V.
Format: Article
Language:English
Subjects:
Amino acids
Amino Acids - chemistry
Animals
Binding sites
Biochemistry
Biological and Medical Physics
Biophysics
Caenorhabditis elegans - metabolism
Caenorhabditis elegans Proteins - chemistry
Double-stranded RNA
Gene expression
Gene regulation
Isoleucine - chemistry
Leucine - chemistry
N.M.R
Nematodes
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Physics
Physics and Astronomy
Polymer Sciences
Protein Structure, Secondary
Proteins
Ribonucleic acid
RNA
RNA Interference
RNA-Binding Proteins - chemistry
RNA-mediated interference
Valine - chemistry
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Summary: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.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-011-9343-0