Publication

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

APA

Sauer, M., Juranek, S. A., Marks, J., De Magis, A., Kazemier, H. G., Hilbig, D., ... Paeschke, K. (2019). DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions. Nature Communications, 10(1), [2421]. https://doi.org/10.1038/s41467-019-10432-5

Author

Sauer, Markus ; Juranek, Stefan A. ; Marks, James ; De Magis, Alessio ; Kazemier, Hinke G. ; Hilbig, Daniel ; Benhalevy, Daniel ; Wang, Xiantao ; Hafner, Markus ; Paeschke, Katrin. / DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions. In: Nature Communications. 2019 ; Vol. 10, No. 1.

Harvard

Sauer, M, Juranek, SA, Marks, J, De Magis, A, Kazemier, HG, Hilbig, D, Benhalevy, D, Wang, X, Hafner, M & Paeschke, K 2019, 'DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions', Nature Communications, vol. 10, no. 1, 2421. https://doi.org/10.1038/s41467-019-10432-5

Standard

DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions. / Sauer, Markus; Juranek, Stefan A.; Marks, James; De Magis, Alessio; Kazemier, Hinke G.; Hilbig, Daniel; Benhalevy, Daniel; Wang, Xiantao; Hafner, Markus; Paeschke, Katrin.

In: Nature Communications, Vol. 10, No. 1, 2421, 03.06.2019.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Sauer M, Juranek SA, Marks J, De Magis A, Kazemier HG, Hilbig D et al. DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions. Nature Communications. 2019 Jun 3;10(1). 2421. https://doi.org/10.1038/s41467-019-10432-5


BibTeX

@article{114e9b0724b74af18ea53094fe836d35,
title = "DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions",
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.",
keywords = "G-QUADRUPLEX STRUCTURES, GENOME-WIDE ANALYSIS, HELICASE RHAU, TETRAMOLECULAR QUADRUPLEX, RESOLVING ACTIVITY, BINDING PROTEIN, MAJOR SOURCE, STRESS, DNA, IDENTIFICATION",
author = "Markus Sauer and Juranek, {Stefan A.} and James Marks and {De Magis}, Alessio and Kazemier, {Hinke G.} and Daniel Hilbig and Daniel Benhalevy and Xiantao Wang and Markus Hafner and Katrin Paeschke",
year = "2019",
month = "6",
day = "3",
doi = "10.1038/s41467-019-10432-5",
language = "English",
volume = "10",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions

AU - Sauer, Markus

AU - Juranek, Stefan A.

AU - Marks, James

AU - De Magis, Alessio

AU - Kazemier, Hinke G.

AU - Hilbig, Daniel

AU - Benhalevy, Daniel

AU - Wang, Xiantao

AU - Hafner, Markus

AU - Paeschke, Katrin

PY - 2019/6/3

Y1 - 2019/6/3

N2 - 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.

AB - 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.

KW - G-QUADRUPLEX STRUCTURES

KW - GENOME-WIDE ANALYSIS

KW - HELICASE RHAU

KW - TETRAMOLECULAR QUADRUPLEX

KW - RESOLVING ACTIVITY

KW - BINDING PROTEIN

KW - MAJOR SOURCE

KW - STRESS

KW - DNA

KW - IDENTIFICATION

U2 - 10.1038/s41467-019-10432-5

DO - 10.1038/s41467-019-10432-5

M3 - Article

VL - 10

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 2421

ER -

ID: 85551731