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Søren Lykke-Andersen

Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors

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Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors. / Falk, Sebastian; Finogenova, Ksenia; Sørensen, Mireille Melko; Benda, Christian; Lykke-Andersen, Søren; Jensen, Torben Heick; Conti, Elena.

I: Nature Communications, Bind 7, 13573, 01.12.2016.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Falk, S, Finogenova, K, Sørensen, MM, Benda, C, Lykke-Andersen, S, Jensen, TH & Conti, E 2016, 'Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors', Nature Communications, bind 7, 13573. https://doi.org/10.1038/ncomms13573

APA

Falk, S., Finogenova, K., Sørensen, M. M., Benda, C., Lykke-Andersen, S., Jensen, T. H., & Conti, E. (2016). Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors. Nature Communications, 7, [13573]. https://doi.org/10.1038/ncomms13573

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Vancouver

Author

Falk, Sebastian ; Finogenova, Ksenia ; Sørensen, Mireille Melko ; Benda, Christian ; Lykke-Andersen, Søren ; Jensen, Torben Heick ; Conti, Elena. / Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors. I: Nature Communications. 2016 ; Bind 7.

Bibtex

@article{a653b40fb1864e82b5b9d4a8c0f9a66f,
title = "Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors",
abstract = "The eukaryotic RNA exosome participates extensively in RNA processing and degradation. In human cells, three accessory factors (RBM7, ZCCHC8 and hMTR4) interact to form the nuclear exosome targeting (NEXT) complex, which directs a subset of non-coding RNAs for exosomal degradation. Here we elucidate how RBM7 is incorporated in the NEXT complex. We identify a proline-rich segment of ZCCHC8 as the interaction site for the RNA-recognition motif (RRM) of RBM7 and present the crystal structure of the corresponding complex at 2.0 {\AA} resolution. On the basis of the structure, we identify a proline-rich segment within the splicing factor SAP145 with strong similarity to ZCCHC8. We show that this segment of SAP145 not only binds the RRM region of another splicing factor SAP49 but also the RRM of RBM7. These dual interactions of RBM7 with the exosome and the spliceosome suggest a model whereby NEXT might recruit the exosome to degrade intronic RNAs.",
author = "Sebastian Falk and Ksenia Finogenova and S{\o}rensen, {Mireille Melko} and Christian Benda and S{\o}ren Lykke-Andersen and Jensen, {Torben Heick} and Elena Conti",
year = "2016",
month = "12",
day = "1",
doi = "10.1038/ncomms13573",
language = "English",
volume = "7",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors

AU - Falk, Sebastian

AU - Finogenova, Ksenia

AU - Sørensen, Mireille Melko

AU - Benda, Christian

AU - Lykke-Andersen, Søren

AU - Jensen, Torben Heick

AU - Conti, Elena

PY - 2016/12/1

Y1 - 2016/12/1

N2 - The eukaryotic RNA exosome participates extensively in RNA processing and degradation. In human cells, three accessory factors (RBM7, ZCCHC8 and hMTR4) interact to form the nuclear exosome targeting (NEXT) complex, which directs a subset of non-coding RNAs for exosomal degradation. Here we elucidate how RBM7 is incorporated in the NEXT complex. We identify a proline-rich segment of ZCCHC8 as the interaction site for the RNA-recognition motif (RRM) of RBM7 and present the crystal structure of the corresponding complex at 2.0 Å resolution. On the basis of the structure, we identify a proline-rich segment within the splicing factor SAP145 with strong similarity to ZCCHC8. We show that this segment of SAP145 not only binds the RRM region of another splicing factor SAP49 but also the RRM of RBM7. These dual interactions of RBM7 with the exosome and the spliceosome suggest a model whereby NEXT might recruit the exosome to degrade intronic RNAs.

AB - The eukaryotic RNA exosome participates extensively in RNA processing and degradation. In human cells, three accessory factors (RBM7, ZCCHC8 and hMTR4) interact to form the nuclear exosome targeting (NEXT) complex, which directs a subset of non-coding RNAs for exosomal degradation. Here we elucidate how RBM7 is incorporated in the NEXT complex. We identify a proline-rich segment of ZCCHC8 as the interaction site for the RNA-recognition motif (RRM) of RBM7 and present the crystal structure of the corresponding complex at 2.0 Å resolution. On the basis of the structure, we identify a proline-rich segment within the splicing factor SAP145 with strong similarity to ZCCHC8. We show that this segment of SAP145 not only binds the RRM region of another splicing factor SAP49 but also the RRM of RBM7. These dual interactions of RBM7 with the exosome and the spliceosome suggest a model whereby NEXT might recruit the exosome to degrade intronic RNAs.

U2 - 10.1038/ncomms13573

DO - 10.1038/ncomms13573

M3 - Journal article

VL - 7

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 13573

ER -