10.6084/m9.figshare.2068551
Annika U. Heininger
Annika
U. Heininger
Philipp Hackert
Philipp
Hackert
Alexandra Z. Andreou
Alexandra
Z. Andreou
Kum-Loong Boon
Kum-Loong
Boon
Indira Memet
Indira
Memet
Mira Prior
Mira
Prior
Anne Clancy
Anne
Clancy
Bernhard Schmidt
Bernhard
Schmidt
Henning Urlaub
Henning
Urlaub
Enrico Schleiff
Enrico
Schleiff
Katherine E. Sloan
Katherine
E. Sloan
Markus Deckers
Markus
Deckers
Reinhard Lührmann
Reinhard
Lührmann
Jörg Enderlein
Jörg
Enderlein
Dagmar Klostermeier
Dagmar
Klostermeier
Peter Rehling
Peter
Rehling
Markus T. Bohnsack
Markus
T. Bohnsack
Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways
Taylor & Francis Group
2016
G-patch protein
ribosome
RNA helicase
splicing
protein cofactor
2016-01-29 08:53:53
Journal contribution
https://tandf.figshare.com/articles/journal_contribution/Protein_cofactor_competition_regulates_the_action_of_a_multifunctional_RNA_helicase_in_different_pathways/2068551
<p>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 suggest that the availability of cofactors and the sequestering of the helicase are means to regulate the activity of multifunctional RNA helicases and their distribution between different cellular processes.</p>