The RNA helicase FRH is an ATP-dependent regulator of CK1a in the circadian clock of Neurospora crassa

The Neurospora clock protein FRQ forms a complex with casein kinase 1a (CK1a) and FRH, a DEAD box-containing RNA helicase with a clock-independent essential function in RNA metabolism. In the course of a circadian period, FRQ is progressively hyperphosphorylated and eventually degraded. Timed hyperp...

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Hauptverfasser: Lauinger, Linda (VerfasserIn) , Diernfellner, Axel (VerfasserIn) , Falk, Sebastian (VerfasserIn) , Brunner, Michael (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 7 Apr 2014
In: Nature Communications
Year: 2014, Jahrgang: 5
ISSN:2041-1723
DOI:10.1038/ncomms4598
Online-Zugang:Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1038/ncomms4598
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/ncomms4598
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Verfasserangaben:Linda Lauinger, Axel Diernfellner, Sebastian Falk & Michael Brunner
Beschreibung
Zusammenfassung:The Neurospora clock protein FRQ forms a complex with casein kinase 1a (CK1a) and FRH, a DEAD box-containing RNA helicase with a clock-independent essential function in RNA metabolism. In the course of a circadian period, FRQ is progressively hyperphosphorylated and eventually degraded. Timed hyperphosphorylation of FRQ is crucial for timekeeping of the clock. Here we show that the ATPase activity of FRH attenuates the kinetics of CK1a-mediated hyperphosphorylation of FRQ. Hyperphosphorylation of FRQ is strictly dependent on site-specific recruitment of a CK1a molecule that is activated upon binding.
Beschreibung:Gesehen am 02.09.2020
Beschreibung:Online Resource
ISSN:2041-1723
DOI:10.1038/ncomms4598