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The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs

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The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs. / Lingaraju, Mahesh; Johnsen, Dennis; Schlundt, Andreas; Langer, Lukas M.; Basquin, Jérôme; Sattler, Michael; Heick Jensen, Torben; Falk, Sebastian; Conti, Elena.

In: Nature Communications, Vol. 10, No. 1, 3393, 12.2019.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Lingaraju, M, Johnsen, D, Schlundt, A, Langer, LM, Basquin, J, Sattler, M, Heick Jensen, T, Falk, S & Conti, E 2019, 'The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs', Nature Communications, vol. 10, no. 1, 3393. https://doi.org/10.1038/s41467-019-11339-x

APA

Lingaraju, M., Johnsen, D., Schlundt, A., Langer, L. M., Basquin, J., Sattler, M., ... Conti, E. (2019). The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs. Nature Communications, 10(1), [3393]. https://doi.org/10.1038/s41467-019-11339-x

CBE

MLA

Vancouver

Lingaraju M, Johnsen D, Schlundt A, Langer LM, Basquin J, Sattler M et al. The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs. Nature Communications. 2019 Dec;10(1). 3393. https://doi.org/10.1038/s41467-019-11339-x

Author

Lingaraju, Mahesh ; Johnsen, Dennis ; Schlundt, Andreas ; Langer, Lukas M. ; Basquin, Jérôme ; Sattler, Michael ; Heick Jensen, Torben ; Falk, Sebastian ; Conti, Elena. / The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs. In: Nature Communications. 2019 ; Vol. 10, No. 1.

Bibtex

@article{0cdfc21d032441fe85cae22b9b6dc202,
title = "The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs",
abstract = "The nuclear exosome and its essential co-factor, the RNA helicase MTR4, play crucial roles in several RNA degradation pathways. Besides unwinding RNA substrates for exosome-mediated degradation, MTR4 associates with RNA-binding proteins that function as adaptors in different RNA processing and decay pathways. Here, we identify and characterize the interactions of human MTR4 with a ribosome processing adaptor, NVL, and with ZCCHC8, an adaptor involved in the decay of small nuclear RNAs. We show that the unstructured regions of NVL and ZCCHC8 contain short linear motifs that bind the MTR4 arch domain in a mutually exclusive manner. These short sequences diverged from the arch-interacting motif (AIM) of yeast rRNA processing factors. Our results suggest that nuclear exosome adaptors have evolved canonical and non-canonical AIM sequences to target human MTR4 and demonstrate the versatility and specificity with which the MTR4 arch domain can recruit a repertoire of different RNA-binding proteins.",
author = "Mahesh Lingaraju and Dennis Johnsen and Andreas Schlundt and Langer, {Lukas M.} and J{\'e}r{\^o}me Basquin and Michael Sattler and {Heick Jensen}, Torben and Sebastian Falk and Elena Conti",
year = "2019",
month = "12",
doi = "10.1038/s41467-019-11339-x",
language = "English",
volume = "10",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs

AU - Lingaraju, Mahesh

AU - Johnsen, Dennis

AU - Schlundt, Andreas

AU - Langer, Lukas M.

AU - Basquin, Jérôme

AU - Sattler, Michael

AU - Heick Jensen, Torben

AU - Falk, Sebastian

AU - Conti, Elena

PY - 2019/12

Y1 - 2019/12

N2 - The nuclear exosome and its essential co-factor, the RNA helicase MTR4, play crucial roles in several RNA degradation pathways. Besides unwinding RNA substrates for exosome-mediated degradation, MTR4 associates with RNA-binding proteins that function as adaptors in different RNA processing and decay pathways. Here, we identify and characterize the interactions of human MTR4 with a ribosome processing adaptor, NVL, and with ZCCHC8, an adaptor involved in the decay of small nuclear RNAs. We show that the unstructured regions of NVL and ZCCHC8 contain short linear motifs that bind the MTR4 arch domain in a mutually exclusive manner. These short sequences diverged from the arch-interacting motif (AIM) of yeast rRNA processing factors. Our results suggest that nuclear exosome adaptors have evolved canonical and non-canonical AIM sequences to target human MTR4 and demonstrate the versatility and specificity with which the MTR4 arch domain can recruit a repertoire of different RNA-binding proteins.

AB - The nuclear exosome and its essential co-factor, the RNA helicase MTR4, play crucial roles in several RNA degradation pathways. Besides unwinding RNA substrates for exosome-mediated degradation, MTR4 associates with RNA-binding proteins that function as adaptors in different RNA processing and decay pathways. Here, we identify and characterize the interactions of human MTR4 with a ribosome processing adaptor, NVL, and with ZCCHC8, an adaptor involved in the decay of small nuclear RNAs. We show that the unstructured regions of NVL and ZCCHC8 contain short linear motifs that bind the MTR4 arch domain in a mutually exclusive manner. These short sequences diverged from the arch-interacting motif (AIM) of yeast rRNA processing factors. Our results suggest that nuclear exosome adaptors have evolved canonical and non-canonical AIM sequences to target human MTR4 and demonstrate the versatility and specificity with which the MTR4 arch domain can recruit a repertoire of different RNA-binding proteins.

UR - http://www.scopus.com/inward/record.url?scp=85069904722&partnerID=8YFLogxK

U2 - 10.1038/s41467-019-11339-x

DO - 10.1038/s41467-019-11339-x

M3 - Journal article

C2 - 31358741

AN - SCOPUS:85069904722

VL - 10

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 3393

ER -