Journal
NUCLEIC ACIDS RESEARCH
Volume 43, Issue 13, Pages 6607-6619Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkv627
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Funding
- Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET) from Argentina [Fellowship]
- Agencia Nacional de Promocion Cientifica y Tecnologica (ANPCyT) from Argentina [PICT-2007-720, PICT-2008-318, PICT-2012-1702]
- Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET) from Argentina [international cooperation grant] [962/2009]
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DCL1 is the ribonuclease that carries out miRNA biogenesis in plants. The enzyme has two tandem double stranded RNA binding domains (dsRBDs) in its C-terminus. Here we show that the first of these domains binds precursor RNA fragments when isolated and cooperates with the second domain in the recognition of substrate RNA. Remarkably, despite showing RNA binding activity, this domain is intrinsically disordered. We found that it acquires a folded conformation when bound to its substrate, being the first report of a complete dsRBD folding upon binding. The free unfolded form shows tendency to adopt folded conformations, and goes through an unfolded bound state prior to the folding event. The significance of these results is discussed by comparison with the behavior of other dsRBDs.
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