Second Double-Stranded RNA Binding Domain of Dicer-like Ribonuclease 1: Structural and Biochemical Characterization
2012; American Chemical Society; Volume: 51; Issue: 51 Linguagem: Inglês
10.1021/bi301247r
ISSN1943-295X
AutoresPaula Burdisso, Irina P. Suárez, Nicolás G. Bologna, Javier F. Palatnik, Beate Bersch, Rodolfo M. Rasia,
Tópico(s)Plant Molecular Biology Research
ResumoDicer-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.
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