6i3r | pdb_00006i3r

Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1/2 of Drosophila helicase MLE

spinqualitylabelsall models 6i3r Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i3r is a 1 chain structure with sequence from Drosophila melanogaster. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MLE_DROME Required in males for dosage compensation of X chromosome linked genes. Mle, msl-1 and msl-3 are colocalized on X chromosome. Each of the msl proteins requires all the other msls for wild-type X-chromosome binding. Probably unwinds double-stranded DNA and RNA in a 3' to 5' direction. Publication Abstract from PubMed Maleless (MLE) is an evolutionary conserved member of the DExH family of helicases in Drosophila. Besides its function in RNA editing and presumably siRNA processing, MLE is best known for its role in remodelling non-coding roX RNA in the context of X chromosome dosage compensation in male flies. MLE and its human orthologue, DHX9 contain two tandem double-stranded RNA binding domains (dsRBDs) located at the N-terminal region. The two dsRBDs are essential for localization of MLE at the X-territory and it is presumed that this involves binding roX secondary structures. However, for dsRBD1 roX RNA binding has so far not been described. Here, we determined the solution NMR structure of dsRBD1 and dsRBD2 of MLE in tandem and investigated its role in double-stranded RNA (dsRNA) binding. Our NMR and SAXS data show that both dsRBDs act as independent structural modules in solution and are canonical, non-sequence-specific dsRBDs featuring non-canonical KKxAXK RNA binding motifs. NMR titrations combined with filter binding experiments and isothermal titration calorimetry (ITC) document the contribution of dsRBD1 to dsRNA binding in vitro. Curiously, dsRBD1 mutants in which dsRNA binding in vitro is strongly compromised do not affect roX2 RNA binding and MLE localization in cells. These data suggest alternative functions for dsRBD1 in vivo. Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless.,Ankush Jagtap PK, Muller M, Masiewicz P, von Bulow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J Nucleic Acids Res. 2019 Feb 26. pii: 5364854. doi: 10.1093/nar/gkz125. PMID:30805612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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