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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Sauer M,Juranek SA,Marks J,De Magis A,Kazemier HG,Hilbig D,Benhalevy D,Wang X,Hafner M,Paeschke Kdoi
10.1038/s41467-019-10432-5subject
Has Abstractpub_date
2019-06-03 00:00:00pages
2421issue
1issn
2041-1723pii
10.1038/s41467-019-10432-5journal_volume
10pub_type
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