Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways

RNA Biology
Annika U HeiningerMarkus T Bohnsack

Abstract

A rapidly increasing number of RNA helicases are implicated in several distinct cellular processes, however, the modes of regulation of multifunctional RNA helicases and their recruitment to different target complexes have remained unknown. Here, we show that the distribution of the multifunctional DEAH-box RNA helicase Prp43 between its diverse cellular functions can be regulated by the interplay of its G-patch protein cofactors. We identify the orphan G-patch protein Cmg1 (YLR271W) as a novel cofactor of Prp43 and show that it stimulates the RNA binding and ATPase activity of the helicase. Interestingly, Cmg1 localizes to the cytoplasm and to the intermembrane space of mitochondria and its overexpression promotes apoptosis. Furthermore, our data reveal that different G-patch protein cofactors compete for interaction with Prp43. Changes in the expression levels of Prp43-interacting G-patch proteins modulate the cellular localization of Prp43 and G-patch protein overexpression causes accumulation of the helicase in the cytoplasm or nucleoplasm. Overexpression of several G-patch proteins also leads to defects in ribosome biogenesis that are consistent with withdrawal of the helicase from this pathway. Together, these findings su...Continue Reading

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Citations

Jan 17, 2017·ELife·Marcel J TauchertRalf Ficner
Mar 5, 2019·Nucleic Acids Research·Florian HamannRalf Ficner
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Apr 16, 2021·Biological Chemistry·Katherine E BohnsackStefanie Jonas
Sep 8, 2018·Journal of Proteome Research·Paula DuekLydie Lane

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Methods Mentioned

BETA
electrophoresis
pulldown
two-hybrid
Fluorescence
fluorescence microscopy
size exclusion chromatography
enzymatic assay

Software Mentioned

ImageQuant
softWoRx
Gene5

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