Identification of a nuclear exosome decay pathway for processed transcripts

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Identification of a nuclear exosome decay pathway for processed transcripts. / Meola, Nicola; Domanski, Michal; Karadoulama, Evdoxia; Chen, Yun; Gentil, Coline Alice Jeanne; Pultz, Dennis; Vitting-Seerup, Kristoffer; Lykke-Andersen, Søren; Andersen, Jens S.; Sandelin, Albin Gustav; Jensen, Torben Heick.

I: Molecular Cell, Bind 64, Nr. 3, 03.11.2016, s. 520-533.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Meola, N, Domanski, M, Karadoulama, E, Chen, Y, Gentil, CAJ, Pultz, D, Vitting-Seerup, K, Lykke-Andersen, S, Andersen, JS, Sandelin, AG & Jensen, TH 2016, 'Identification of a nuclear exosome decay pathway for processed transcripts', Molecular Cell, bind 64, nr. 3, s. 520-533. https://doi.org/10.1016/j.molcel.2016.09.025

APA

Meola, N., Domanski, M., Karadoulama, E., Chen, Y., Gentil, C. A. J., Pultz, D., Vitting-Seerup, K., Lykke-Andersen, S., Andersen, J. S., Sandelin, A. G., & Jensen, T. H. (2016). Identification of a nuclear exosome decay pathway for processed transcripts. Molecular Cell, 64(3), 520-533. https://doi.org/10.1016/j.molcel.2016.09.025

Vancouver

Meola N, Domanski M, Karadoulama E, Chen Y, Gentil CAJ, Pultz D o.a. Identification of a nuclear exosome decay pathway for processed transcripts. Molecular Cell. 2016 nov. 3;64(3):520-533. https://doi.org/10.1016/j.molcel.2016.09.025

Author

Meola, Nicola ; Domanski, Michal ; Karadoulama, Evdoxia ; Chen, Yun ; Gentil, Coline Alice Jeanne ; Pultz, Dennis ; Vitting-Seerup, Kristoffer ; Lykke-Andersen, Søren ; Andersen, Jens S. ; Sandelin, Albin Gustav ; Jensen, Torben Heick. / Identification of a nuclear exosome decay pathway for processed transcripts. I: Molecular Cell. 2016 ; Bind 64, Nr. 3. s. 520-533.

Bibtex

@article{58b9202392c545168abb56d1a5bb731b,

title = "Identification of a nuclear exosome decay pathway for processed transcripts",

abstract = "The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its co-factor Mtr4p/hMTR4, which links to RNA-binding protein adaptors. One example is the trimeric human nuclear exosome targeting (NEXT) complex, which is composed of hMTR4, the Zn-finger protein ZCCHC8, and the RNA-binding factor RBM7. NEXT primarily targets early and unprocessed transcripts, which demands a rationale for how the nuclear exosome recognizes processed RNAs. Here, we describe the poly(A) tail exosome targeting (PAXT) connection, which comprises the ZFC3H1 Zn-knuckle protein as a central link between hMTR4 and the nuclear poly(A)-binding protein PABPN1. Individual depletion of ZFC3H1 and PABPN1 results in the accumulation of common transcripts that are generally both longer and more extensively polyadenylated than NEXT substrates. Importantly, ZFC3H1/PABPN1 and ZCCHC8/RBM7 contact hMTR4 in a mutually exclusive manner, revealing that the exosome targets nuclear transcripts of different maturation status by substituting its hMTR4-associating adaptors.",

author = "Nicola Meola and Michal Domanski and Evdoxia Karadoulama and Yun Chen and Gentil, {Coline Alice Jeanne} and Dennis Pultz and Kristoffer Vitting-Seerup and S{\o}ren Lykke-Andersen and Andersen, {Jens S.} and Sandelin, {Albin Gustav} and Jensen, {Torben Heick}",

year = "2016",

month = nov,

day = "3",

doi = "10.1016/j.molcel.2016.09.025",

language = "English",

volume = "64",

pages = "520--533",

journal = "Molecular Cell",

issn = "1097-2765",

publisher = "Cell Press",

number = "3",

}

RIS

TY - JOUR

T1 - Identification of a nuclear exosome decay pathway for processed transcripts

AU - Meola, Nicola

AU - Domanski, Michal

AU - Karadoulama, Evdoxia

AU - Chen, Yun

AU - Gentil, Coline Alice Jeanne

AU - Pultz, Dennis

AU - Vitting-Seerup, Kristoffer

AU - Lykke-Andersen, Søren

AU - Andersen, Jens S.

AU - Sandelin, Albin Gustav

AU - Jensen, Torben Heick

PY - 2016/11/3

Y1 - 2016/11/3

N2 - The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its co-factor Mtr4p/hMTR4, which links to RNA-binding protein adaptors. One example is the trimeric human nuclear exosome targeting (NEXT) complex, which is composed of hMTR4, the Zn-finger protein ZCCHC8, and the RNA-binding factor RBM7. NEXT primarily targets early and unprocessed transcripts, which demands a rationale for how the nuclear exosome recognizes processed RNAs. Here, we describe the poly(A) tail exosome targeting (PAXT) connection, which comprises the ZFC3H1 Zn-knuckle protein as a central link between hMTR4 and the nuclear poly(A)-binding protein PABPN1. Individual depletion of ZFC3H1 and PABPN1 results in the accumulation of common transcripts that are generally both longer and more extensively polyadenylated than NEXT substrates. Importantly, ZFC3H1/PABPN1 and ZCCHC8/RBM7 contact hMTR4 in a mutually exclusive manner, revealing that the exosome targets nuclear transcripts of different maturation status by substituting its hMTR4-associating adaptors.

AB - The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its co-factor Mtr4p/hMTR4, which links to RNA-binding protein adaptors. One example is the trimeric human nuclear exosome targeting (NEXT) complex, which is composed of hMTR4, the Zn-finger protein ZCCHC8, and the RNA-binding factor RBM7. NEXT primarily targets early and unprocessed transcripts, which demands a rationale for how the nuclear exosome recognizes processed RNAs. Here, we describe the poly(A) tail exosome targeting (PAXT) connection, which comprises the ZFC3H1 Zn-knuckle protein as a central link between hMTR4 and the nuclear poly(A)-binding protein PABPN1. Individual depletion of ZFC3H1 and PABPN1 results in the accumulation of common transcripts that are generally both longer and more extensively polyadenylated than NEXT substrates. Importantly, ZFC3H1/PABPN1 and ZCCHC8/RBM7 contact hMTR4 in a mutually exclusive manner, revealing that the exosome targets nuclear transcripts of different maturation status by substituting its hMTR4-associating adaptors.

U2 - 10.1016/j.molcel.2016.09.025

DO - 10.1016/j.molcel.2016.09.025

M3 - Journal article

C2 - 27871484

VL - 64

SP - 520

EP - 533

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 3

ER -

ID: 169385497

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