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

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Schlagwörter: CHROMOSOME DOSAGE COMPENSATION; X-CHROMOSOME; MSL COMPLEX; CRYSTAL-STRUCTURE; NONCODING RNA; DROSOPHILA MALELESS; BINDING DOMAINS; PROTEINS; ASSOCIATION; ROX1
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2015
 Publikationsstatus: Erschienen
 Seiten: 13
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000368286000017
DOI: 10.1016/j.molcel.2015.10.011
 Art des Abschluß: -

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Titel: MOLECULAR CELL
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Seiten: - Band / Heft: 60 (3) Artikelnummer: - Start- / Endseite: 487 - 499 Identifikator: ISSN: 1097-2765