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PXD045725-1

PXD045725 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleStructural basis of RNA-induced autoregulation of the DExH-type RNA helicase maleless
DescriptionRNA unwinding by DExH-type helicases underlies most RNA metabolism and function. It remains unresolved if and how the basic unwinding reaction of helicases is regulated by auxiliary domains. We explored the interplay between the RecA and auxiliary domains of the RNA helicase maleless (MLE) from Drosophila, using a suite of structural and functional studies. We discovered that MLE exists in a dsRNA bound open conformation and the auxiliary dsRBD2 domain aligns the substrate RNA with the accessible helicase tunnel. In an ATP-dependent manner, dsRBD2 associates with the helicase module, leading to tunnel closure around ssRNA. Furthermore, our structures provide a rationale for blunt ended dsRNA unwinding and 3’-5’ translocation by MLE. Structure-based MLE mutations confirm the functional relevance of our model for RNA unwinding. Our findings contribute to our understanding of fundamental mechanics of auxiliary domains in DExH helicase MLE which serves as model for its human ortholog and potentially therapeutic target, DHX9/RHA.
HostingRepositoryPRIDE
AnnounceDate2023-11-27
AnnouncementXMLSubmission_2023-11-27_01:26:26.190.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAnna Kiss
SpeciesList scientific name: Drosophila melanogaster (Fruit fly); NCBI TaxID: 7227;
ModificationListNo PTMs are included in the dataset
InstrumentQ Exactive HF
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-09-27 01:41:55ID requested
12023-11-27 01:26:26announced
22024-10-22 06:15:53announced2024-10-22: Updated project metadata.
Publication List
10.1016/J.MOLCEL.2023.10.026;
Keyword List
submitter keyword: Helicase, QexactiveHF, CL-MS, MLE, RNA, CX-MS, crosslinking, Drosophila melanogaster
Contact List
Janosch Hennig
contact affiliation1) Structural and Computational Biology Unit, EMBL Heidelberg, Meyerhofstraße 1, 69117, Heidelberg, Germany 2) Chair of Biochemistry IV, Biophysical Chemistry, University of Bayreuth, Bayreuth, Germany
contact emailjanosch.hennig@embl.de
lab head
Anna Kiss
contact affiliationLudwig-Maximilians-Universität, München
contact emailanna.kiss@bmc.med.lmu.de
dataset submitter
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Dataset FTP location
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PRIDE project URI
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