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Article

Structure of RDE-4 dsRBDs and mutational studies provide insights into dsRNA recognition in the Caenorhabditis elegans RNAi pathway.

The Biochemical journal - 15 Feb 2014

Chiliveri Sai Chaitanya, Deshmukh Mandar V

Abstract excerpt

The association of RDE-4 (RNAi defective 4), a protein containing two dsRBDs (dsRNA-binding domains), with long dsRNA and Dcr-1 (Dicer1 homologue) initiates the siRNA pathway in Caenorhabditis elegans. Unlike its homologues in higher eukaryotes, RDE-4 dsRBDs possess weak (micromolar) affinity for short dsRNA. With increasing length of dsRNA, RDE-4 exhibits enhanced affinity due to co-operativity. The linker and...

Topics

Animals
Base Sequence
Caenorhabditis elegans
DNA
DNA Primers
Magnetic Resonance Spectroscopy
Mutagenesis, Site-Directed
Mutation
RNA Interference

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 24256178
DOI: 10.1042/BJ20131347

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