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

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

    865 Downloads (Pure)

    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.
    Original languageEnglish
    JournalNature Structural and Molecular Biology
    Volume20
    Issue12
    Pages (from-to)1358-1366
    Number of pages9
    ISSN1545-9993
    DOIs
    Publication statusPublished - 24 Nov 2013

    Fingerprint

    Dive into the research topics of 'CBC-ARS2 stimulates 3'-end maturation of multiple RNA families and favors cap-proximal processing'. Together they form a unique fingerprint.

    Cite this