CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing

Marie Hallais; Frédéric Pontvianne; Peter Refsing Andersen; Marcello Clerici; Daniela Lener; Nour El Houda Benbahouche; Thierry Gostan; Franck Vandermoere; Marie-Cécile Robert; Stephen Cusack; Céline Verheggen; Torben Heick Jensen; Edouard Bertrand

doi:10.1038/nsmb.2720

CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing

Marie Hallais, Frédéric Pontvianne, Peter Refsing Andersen, Marcello Clerici, Daniela Lener, Nour El Houda Benbahouche, Thierry Gostan, Franck Vandermoere, Marie-Cécile Robert, Stephen Cusack, Céline Verheggen, Torben Heick Jensen, Edouard Bertrand

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

132 Citationer (Scopus)

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Abstract

The nuclear cap-binding complex (CBC) stimulates multiple steps in several RNA maturation pathways, but how it functions in humans is incompletely understood. For small, capped RNAs such as pre-snRNAs, the CBC recruits PHAX. Here, we identify the CBCAP complex, composed of CBC, ARS2 and PHAX, and show that both CBCAP and CBC-ARS2 complexes can be reconstituted from recombinant proteins. ARS2 stimulates PHAX binding to the CBC and snRNA 3'-end processing, thereby coupling maturation with export. In vivo, CBC and ARS2 bind similar capped noncoding and coding RNAs and stimulate their 3'-end processing. The strongest effects are for cap-proximal polyadenylation sites, and this favors premature transcription termination. ARS2 functions partly through the mRNA 3'-end cleavage factor CLP1, which binds RNA Polymerase II through PCF11. ARS2 is thus a major CBC effector that stimulates functional and cryptic 3'-end processing sites.

Originalsprog	Engelsk
Tidsskrift	Nature Structural and Molecular Biology
Vol/bind	20
Nummer	12
Sider (fra-til)	1358-1366
Antal sider	9
ISSN	1545-9993
DOI	https://doi.org/10.1038/nsmb.2720
Status	Udgivet - 24 nov. 2013

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10.1038/nsmb.2720

Hallais et al. 2013

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Hallais, M., Pontvianne, F., Andersen, P. R., Clerici, M., Lener, D., Benbahouche, N. E. H., Gostan, T., Vandermoere, F., Robert, M.-C., Cusack, S., Verheggen, C., Jensen, T. H., & Bertrand, E. (2013). CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing. Nature Structural and Molecular Biology, 20(12), 1358-1366. https://doi.org/10.1038/nsmb.2720

@article{6fed95f930c146f6bbe55097eb64d861,

title = "CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing",

abstract = "The nuclear cap-binding complex (CBC) stimulates multiple steps in several RNA maturation pathways, but how it functions in humans is incompletely understood. For small, capped RNAs such as pre-snRNAs, the CBC recruits PHAX. Here, we identify the CBCAP complex, composed of CBC, ARS2 and PHAX, and show that both CBCAP and CBC-ARS2 complexes can be reconstituted from recombinant proteins. ARS2 stimulates PHAX binding to the CBC and snRNA 3'-end processing, thereby coupling maturation with export. In vivo, CBC and ARS2 bind similar capped noncoding and coding RNAs and stimulate their 3'-end processing. The strongest effects are for cap-proximal polyadenylation sites, and this favors premature transcription termination. ARS2 functions partly through the mRNA 3'-end cleavage factor CLP1, which binds RNA Polymerase II through PCF11. ARS2 is thus a major CBC effector that stimulates functional and cryptic 3'-end processing sites.",

author = "Marie Hallais and Fr{\'e}d{\'e}ric Pontvianne and Andersen, {Peter Refsing} and Marcello Clerici and Daniela Lener and Benbahouche, {Nour El Houda} and Thierry Gostan and Franck Vandermoere and Marie-C{\'e}cile Robert and Stephen Cusack and C{\'e}line Verheggen and Jensen, {Torben Heick} and Edouard Bertrand",

year = "2013",

month = nov,

day = "24",

doi = "10.1038/nsmb.2720",

language = "English",

volume = "20",

pages = "1358--1366",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "Nature Research",

number = "12",

}

Hallais, M, Pontvianne, F, Andersen, PR, Clerici, M, Lener, D, Benbahouche, NEH, Gostan, T, Vandermoere, F, Robert, M-C, Cusack, S, Verheggen, C, Jensen, TH & Bertrand, E 2013, 'CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing', Nature Structural and Molecular Biology, bind 20, nr. 12, s. 1358-1366. https://doi.org/10.1038/nsmb.2720

CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing. / Hallais, Marie; Pontvianne, Frédéric; Andersen, Peter Refsing et al.
I: Nature Structural and Molecular Biology, Bind 20, Nr. 12, 24.11.2013, s. 1358-1366.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

TY - JOUR

T1 - CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing

AU - Hallais, Marie

AU - Pontvianne, Frédéric

AU - Andersen, Peter Refsing

AU - Clerici, Marcello

AU - Lener, Daniela

AU - Benbahouche, Nour El Houda

AU - Gostan, Thierry

AU - Vandermoere, Franck

AU - Robert, Marie-Cécile

AU - Cusack, Stephen

AU - Verheggen, Céline

AU - Jensen, Torben Heick

AU - Bertrand, Edouard

PY - 2013/11/24

Y1 - 2013/11/24

N2 - The nuclear cap-binding complex (CBC) stimulates multiple steps in several RNA maturation pathways, but how it functions in humans is incompletely understood. For small, capped RNAs such as pre-snRNAs, the CBC recruits PHAX. Here, we identify the CBCAP complex, composed of CBC, ARS2 and PHAX, and show that both CBCAP and CBC-ARS2 complexes can be reconstituted from recombinant proteins. ARS2 stimulates PHAX binding to the CBC and snRNA 3'-end processing, thereby coupling maturation with export. In vivo, CBC and ARS2 bind similar capped noncoding and coding RNAs and stimulate their 3'-end processing. The strongest effects are for cap-proximal polyadenylation sites, and this favors premature transcription termination. ARS2 functions partly through the mRNA 3'-end cleavage factor CLP1, which binds RNA Polymerase II through PCF11. ARS2 is thus a major CBC effector that stimulates functional and cryptic 3'-end processing sites.

AB - The nuclear cap-binding complex (CBC) stimulates multiple steps in several RNA maturation pathways, but how it functions in humans is incompletely understood. For small, capped RNAs such as pre-snRNAs, the CBC recruits PHAX. Here, we identify the CBCAP complex, composed of CBC, ARS2 and PHAX, and show that both CBCAP and CBC-ARS2 complexes can be reconstituted from recombinant proteins. ARS2 stimulates PHAX binding to the CBC and snRNA 3'-end processing, thereby coupling maturation with export. In vivo, CBC and ARS2 bind similar capped noncoding and coding RNAs and stimulate their 3'-end processing. The strongest effects are for cap-proximal polyadenylation sites, and this favors premature transcription termination. ARS2 functions partly through the mRNA 3'-end cleavage factor CLP1, which binds RNA Polymerase II through PCF11. ARS2 is thus a major CBC effector that stimulates functional and cryptic 3'-end processing sites.

U2 - 10.1038/nsmb.2720

DO - 10.1038/nsmb.2720

M3 - Journal article

C2 - 24270878

SN - 1545-9993

VL - 20

SP - 1358

EP - 1366

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 12

ER -

CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing

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