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

Sauer, M., Juranek, S. A., Marks, J., De Magis, A., Kazemier, H. G., Hilbig, D., Benhalevy, D., Wang, X., Hafner, M. & Paeschke, K., 3-Jun-2019, In : Nature Communications. 10, 1, 15 p., 2421.

Research output: Contribution to journalArticleAcademicpeer-review

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.

Original languageEnglish
Article number2421
Number of pages15
JournalNature Communications
Volume10
Issue number1
Publication statusPublished - 3-Jun-2019

    Keywords

  • G-QUADRUPLEX STRUCTURES, GENOME-WIDE ANALYSIS, HELICASE RHAU, TETRAMOLECULAR QUADRUPLEX, RESOLVING ACTIVITY, BINDING PROTEIN, MAJOR SOURCE, STRESS, DNA, IDENTIFICATION

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