2lrs

Publication Abstract from PubMed

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.

Second Double-Stranded RNA Binding Domain of Dicer-like Ribonuclease 1: Structural and Biochemical Characterization.,Burdisso P, Suarez IP, Bologna NG, Palatnik JF, Bersch B, Rasia RM Biochemistry. 2012 Dec 21;51(51):10159-66. doi: 10.1021/bi301247r. Epub 2012 Dec , 12. PMID:23194006^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.