|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1/2 of Drosophila helicase MLE== | | ==Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1/2 of Drosophila helicase MLE== |
| - | <StructureSection load='6i3r' size='340' side='right'caption='[[6i3r]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='6i3r' size='340' side='right'caption='[[6i3r]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6i3r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I3R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6i3r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I3R FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mle, nap, CG11680 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6i3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i3r OCA], [https://pdbe.org/6i3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i3r RCSB], [https://www.ebi.ac.uk/pdbsum/6i3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i3r ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6i3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i3r OCA], [http://pdbe.org/6i3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i3r RCSB], [http://www.ebi.ac.uk/pdbsum/6i3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i3r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MLE_DROME 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.<ref>PMID:1653648</ref> | + | [https://www.uniprot.org/uniprot/MLE_DROME 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.<ref>PMID:1653648</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RNA helicase]]
| + | [[Category: Buelow Sv]] |
| - | [[Category: Buelow, S v]] | + | [[Category: Hennig J]] |
| - | [[Category: Hennig, J]] | + | [[Category: Jagtap PKA]] |
| - | [[Category: Jagtap, P K.A]] | + | [[Category: Masiewicz P]] |
| - | [[Category: Masiewicz, P]] | + | [[Category: Simon B]] |
| - | [[Category: Simon, B]] | + | |
| - | [[Category: Dsrbd]]
| + | |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| Structural highlights
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuroda MI, Kernan MJ, Kreber R, Ganetzky B, Baker BS. The maleless protein associates with the X chromosome to regulate dosage compensation in Drosophila. Cell. 1991 Sep 6;66(5):935-47. PMID:1653648
- ↑ Ankush Jagtap PK, Muller M, Masiewicz P, von Bulow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J. Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res. 2019 Feb 26. pii: 5364854. doi: 10.1093/nar/gkz125. PMID:30805612 doi:http://dx.doi.org/10.1093/nar/gkz125
|
