期刊
MOLECULAR CELL
卷 60, 期 3, 页码 487-499出版社
CELL PRESS
DOI: 10.1016/j.molcel.2015.10.011
关键词
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资金
- Max Planck Gesellschaft
- European Commission (ERC, Marie Curie ITN RNPnet) [294371, 293948]
- Deutsche Forschungsgemeinschaft [DFG SFB646, SFB1035, GRK1721, FOR1680]
- European Research Council (ERC) [293948, 294371] Funding Source: European Research Council (ERC)
The MLE helicase remodels the roX lncRNAs, enabling the lncRNA-mediated assembly of the Drosophila dosage compensation complex. We identified a stable MLE core comprising the DExH helicase module and two auxiliary domains: a dsRBD and an OB-like fold. MLEcore is an unusual DExH helicase that can unwind blunt-ended RNA duplexes and has specificity for uridine nucleotides. We determined the 2.1 angstrom resolution structure of MLEcore bound to a U10RNA and ADP-AlF4. The OB-like and dsRBD folds bind the DExH module and contribute to form the entrance of the helicase channel. Four uridine nucleotides engage in base-specific interactions, rationalizing the conservation of uridine-rich sequences in critical roX substrates. roX2 binding is orchestrated by MLE's auxiliary domains, which is prerequisite for MLE localization to the male X chromosome. The structure visualizes a transition-state mimic of the reaction and suggests how eukaryotic DEAH/RHA heli-cases couple ATP hydrolysis to RNA translocation.
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