DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions

Markus Sauer, Stefan A. Juranek, James Marks, Alessio Magis, Hinke G. Kazemier, Daniel Hilbig, Daniel Benhalevy, Xiantao Wang, Markus Hafner () and Katrin Paeschke ()
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Markus Sauer: University of Würzburg
Stefan A. Juranek: University Hospital Bonn
James Marks: National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIH
Alessio Magis: University Hospital Bonn
Hinke G. Kazemier: University of Groningen
Daniel Hilbig: University Hospital Bonn
Daniel Benhalevy: National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIH
Xiantao Wang: National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIH
Markus Hafner: National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIH
Katrin Paeschke: University of Würzburg

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract Translation efficiency can be affected by mRNA stability and secondary structures, including G-quadruplex structures (G4s). The highly conserved DEAH-box helicase DHX36/RHAU resolves G4s on DNA and RNA in vitro, however a systems-wide analysis of DHX36 targets and function is lacking. We map globally DHX36 binding to RNA in human cell lines and find it preferentially interacting with G-rich and G4-forming sequences on more than 4500 mRNAs. While DHX36 knockout (KO) results in a significant increase in target mRNA abundance, ribosome occupancy and protein output from these targets decrease, suggesting that they were rendered translationally incompetent. Considering that DHX36 targets, harboring G4s, preferentially localize in stress granules, and that DHX36 KO results in increased SG formation and protein kinase R (PKR/EIF2AK2) phosphorylation, we speculate that DHX36 is involved in resolution of rG4 induced cellular stress.

Date: 2019
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DOI: 10.1038/s41467-019-10432-5

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