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  Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling

Prabu, J. R., Müller, M., Thomae, A. W., Schüssler, S., Bonneau, F., Becker, P. B., et al. (2015). Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. MOLECULAR CELL, 60(3), 487-499. doi:10.1016/j.molcel.2015.10.011.

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 Creators:
Prabu, J. Rajan1, Author              
Müller, Marisa2, Author
Thomae, Andreas W.2, Author
Schüssler, Steffen1, Author              
Bonneau, Fabien1, Author              
Becker, Peter B.2, Author
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2external, ou_persistent22              

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Free keywords: CHROMOSOME DOSAGE COMPENSATION; X-CHROMOSOME; MSL COMPLEX; CRYSTAL-STRUCTURE; NONCODING RNA; DROSOPHILA MALELESS; BINDING DOMAINS; PROTEINS; ASSOCIATION; ROX1
 Abstract: 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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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: MOLECULAR CELL
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 60 (3) Sequence Number: - Start / End Page: 487 - 499 Identifier: ISSN: 1097-2765