1. Second double-stranded RNA binding domain of dicer-like ribonuclease 1: structural and biochemical characterization.
- Author
-
Burdisso P, Suarez IP, Bologna NG, Palatnik JF, Bersch B, and Rasia RM
- Subjects
- Arabidopsis enzymology, Arabidopsis Proteins metabolism, Cell Cycle Proteins metabolism, DEAD-box RNA Helicases chemistry, DNA metabolism, MicroRNAs metabolism, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary, Arabidopsis Proteins chemistry, Cell Cycle Proteins chemistry, RNA, Double-Stranded metabolism, Ribonuclease III chemistry, Ribonuclease III metabolism
- Abstract
Dicer-like ribonuclease III enzymes are involved in different paths related to RNA silencing in plants. Little is known about the structural aspects of these processes. Here we present a structural characterization of the second double-stranded RNA binding domain (dsRBD) of DCL1, which is presumed to participate in pri-micro-RNA recognition and subcellular localization of this protein. We determined the solution structure and found that it has a canonical fold but bears some variation with respect to other homologous domains. We also found that this domain binds both double-stranded RNA and double-stranded DNA, in contrast to most dsRBDs. Our characterization shows that this domain likely has functions other than substrate recognition and binding.
- Published
- 2012
- Full Text
- View/download PDF