Induced folding in RNA recognition by Arabidopsis thaliana DCL1.

Autor:	Suarez IP; Instituto de Biología Molecular y Celular de Rosario. 27 de Febrero 210 bis, predio CCT, 2000 Rosario, Argentina Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Suipacha 531, 2000 Rosario, Argentina., Burdisso P; Instituto de Biología Molecular y Celular de Rosario. 27 de Febrero 210 bis, predio CCT, 2000 Rosario, Argentina Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Suipacha 531, 2000 Rosario, Argentina., Benoit MP; CEA, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France CNRS, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France Université Joseph Fourier - Grenoble 1, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France., Boisbouvier J; CEA, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France CNRS, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France Université Joseph Fourier - Grenoble 1, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France., Rasia RM; Instituto de Biología Molecular y Celular de Rosario. 27 de Febrero 210 bis, predio CCT, 2000 Rosario, Argentina Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Suipacha 531, 2000 Rosario, Argentina rasia@ibr-conicet.gov.ar.
Jazyk:	angličtina
Zdroj:	Nucleic acids research [Nucleic Acids Res] 2015 Jul 27; Vol. 43 (13), pp. 6607-19. Date of Electronic Publication: 2015 Jun 22.
DOI:	10.1093/nar/gkv627
Abstrakt:	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. (© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Databáze:	MEDLINE
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