Second Double-Stranded RNA Binding Domain of Dicer-like Ribonuclease 1: Structural and Biochemical Characterization

BURDISSO PAULA; SUAREZ IRINA PAULA; BOLOGNA NICOLÁS; PALATNIK JAVIER; BERSCH BEATE; RASIA RODOLFO

BIOCHEMISTRY

AMER CHEMICAL SOC

Lugar: Washington; Año: 2012 vol. 51 p. 10159 - 10166

0006-2960

Dicer-like ribonuclease III enzymes are involvedin 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 seconddouble-stranded RNA binding domain (dsRBD) of DCL1,which is presumed to participate in pri-micro-RNA recognitionand subcellular localization of this protein. We determined thesolution structure and found that it has a canonical fold butbears some variation with respect to other homologousdomains. We also found that this domain binds both doublestrandedRNA and double-stranded DNA, in contrast to mostdsRBDs. Our characterization shows that this domain likely has functions other than substrate recognition and binding.