Induced folding in RNA recognition by Arabidopsis thaliana DCL1
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Oxford University Press
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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.
This article has been accepted for publication in Nucleic Acids Research Published by Oxford University Press.
This article has been accepted for publication in Nucleic Acids Research Published by Oxford University Press.
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