title: Induced folding in RNA recognition by Arabidopsis thaliana DCL1.
abstract: 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.
authors.affiliation: 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.
authors.forename: Irina P
authors.initials: IP
authors.lastname: Suarez
authors.affiliation: 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.
authors.forename: Paula
authors.initials: P
authors.lastname: Burdisso
authors.affiliation: 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.
authors.forename: Matthieu P M H
authors.initials: MP
authors.lastname: Benoit
authors.affiliation: 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.
authors.forename: Jèrôme
authors.initials: J
authors.lastname: Boisbouvier
authors.affiliation: 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.
authors.forename: Rodolfo M
authors.initials: RM
authors.lastname: Rasia
mesh_terms: D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism; D064267:Intrinsically Disordered Proteins / Q000737:chemistry; D008958:Models, Molecular; D011485:Protein Binding; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D059370:RNA Folding; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D043244:Ribonuclease III / Q000737:chemistry* / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D018797:Cell Cycle Proteins; D064267:Intrinsically Disordered Proteins; D016601:RNA-Binding Proteins; D012313:RNA; C402383:DCL1 protein, Arabidopsis; D043244:Ribonuclease III