Rde 4 sandbox: Difference between revisions
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RDE-4 was identified through a genome-wide screening as a gene responsible for greatly reducing or abolishing RNAi in C. elegans. In organisms ranging from Arabidopsis to humans, Dicer requires dsRNA-binding proteins (dsRBPs) to carry out its roles in RNA interference (RNAi) and micro-RNA (miRNA) processing. In Caenorhabditis elegans, the dsRBP RDE-4 acts with Dicer during the initiation of RNAi, when long dsRNA is cleaved to small interfering RNAs (siRNAs). RDE-4 is not sequence-specific, however, RDE-4 binds with higher affinity to long dsRNA. Interestingly, RDE- 4 is the only protein that exhibits micromolar affinity for dsRNA in the absence of co-operativity. In addition, RDE-4 is a homodimer in solution. <ref name=first>DOI: 10.1261/rna.2338706</ref> (Yellow Citation) | RDE-4 was identified through a genome-wide screening as a gene responsible for greatly reducing or abolishing RNAi in C. elegans. In organisms ranging from Arabidopsis to humans, Dicer requires dsRNA-binding proteins (dsRBPs) to carry out its roles in RNA interference (RNAi) and micro-RNA (miRNA) processing. In Caenorhabditis elegans, the dsRBP RDE-4 acts with Dicer during the initiation of RNAi, when long dsRNA is cleaved to small interfering RNAs (siRNAs). RDE-4 is not sequence-specific, however, RDE-4 binds with higher affinity to long dsRNA. Interestingly, RDE- 4 is the only protein that exhibits micromolar affinity for dsRNA in the absence of co-operativity. In addition, RDE-4 is a homodimer in solution. <ref name=first>DOI: 10.1261/rna.2338706</ref> (Yellow Citation) | ||
<Structure load=' | <Structure load='2LTS' size='350' frame='true' align='right' caption='Structure of RDE-4 (pdb code 2LTS)'/> | ||
<Structure load=' | <Structure load='2LTR' size='350' frame='true' align='right' caption='Structure of RDE-4 (pdb code 2LTR)'/> | ||
== Structure of RDE-4 == | == Structure of RDE-4 == | ||
