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doi:10.22028/D291-43475
Titel: | Molecular simulations of DEAH-box helicases reveal control of domain flexibility by ligands: RNA, ATP, ADP, and G-patch proteins |
VerfasserIn: | Becker, Robert A. Hub, Jochen Sebastian |
Sprache: | Englisch |
Titel: | Biological chemistry |
Bandnummer: | 404 |
Heft: | 8-9 |
Seiten: | 867–879 |
Verlag/Plattform: | De Gruyter |
Erscheinungsjahr: | 2023 |
Freie Schlagwörter: | DEAH-box helicases G-patch molecular dynamics simulations simulated tempering |
DDC-Sachgruppe: | 500 Naturwissenschaften |
Dokumenttyp: | Journalartikel / Zeitschriftenartikel |
Abstract: | DEAH-box helicases use the energy from ATP hydrolysis to translocate along RNA strands. They are composed of tandem RecA-like domains and a C-terminal domain connected by flexible linkers, and the activity of several DEAH-box helicases is regulated by cofactors called G-patch proteins. We used all-atom molecular dynamics simulations of the helicases Prp43, Prp22, and DHX15 in various liganded states to investigate how RNA, ADP, ATP, or G-patch proteins influence their conformational dynamics. The simulations suggest that apo helicases are highly flexible, whereas binding of RNA renders the helicases more rigid. ATP and ADP control the stability of the RecA1-RecA2 interface, but they have only a smaller effect on domain flexibility in absence of a RecA1-RecA2 interface. Binding of a G-patch protein to DHX15 imposes a more structured conformational ensemble, characterized by more defined relative domain arrangements and by an increased conformational stability of the RNA tunnel. However, the effect of the G-patch protein on domain dynamics is far more subtle as compared to the effects of RNA or ATP/ADP. The simulations characterize DEAH-box helicase as dynamic machines whose conformational ensembles are strongly defined by the presence of RNA, ATP, or ADP and only fine-tuned by the presence of G-patch proteins. |
DOI der Erstveröffentlichung: | 10.1515/hsz-2023-0154 |
URL der Erstveröffentlichung: | https://www.degruyter.com/document/doi/10.1515/hsz-2023-0154/html |
Link zu diesem Datensatz: | urn:nbn:de:bsz:291--ds-434758 hdl:20.500.11880/38978 http://dx.doi.org/10.22028/D291-43475 |
ISSN: | 1437-4315 1431-6730 |
Datum des Eintrags: | 18-Nov-2024 |
Fakultät: | NT - Naturwissenschaftlich- Technische Fakultät |
Fachrichtung: | NT - Physik |
Professur: | NT - Prof. Dr. Jochen Hub |
Sammlung: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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10.1515_hsz-2023-0154.pdf | 3,78 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons