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Sharma, P.* ; Lioutas, A.* ; Fernandez-Fuentes, N.* ; Quilez, J.* ; Carbonell-Caballero, J.* ; Wright, R.H.G.* ; Di Vona, C.* ; Le Dily, F.* ; Schüller, R. ; Eick, D. ; Oliva, B.* ; Beato, M.*

Arginine citrullination at the C-terminal domain controls RNA polymerase II transcription.

Mol. Cell 73, 84-96 (2018)
Verlagsversion DOI
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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The post-translational modification of key residues at the C-terminal domain of RNA polymerase II (RNAP2-CTD) coordinates transcription, splicing, and RNA processing by modulating its capacity to act as a landing platform for a variety of protein complexes. Here, we identify a new modification at the CTD, the deimination of arginine and its conversion to citrulline by peptidyl arginine deiminase 2 (PADI2), an enzyme that has been associated with several diseases, including cancer. We show that, among PADI family members, only PADI2 citrullinates R1810 (Cit1810) at repeat 31 of the CTD. Depletion of PADI2 or loss of R1810 results in accumulation of RNAP2 at transcription start sites, reduced gene expression, and inhibition of cell proliferation. Cit1810 is needed for interaction with the P-TEFb (positive transcription elongation factor b) kinase complex and for its recruitment to chromatin. In this way, CTD-Cit1810 favors RNAP2 pause release and efficient transcription in breast cancer cells.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Arginine1810 ; Breast Cancer Cells ; Cell Proliferation ; Citrullination ; P-tefb Complex ; Padi2 ; Proximal Promoter Pausing ; Rna Polymerase Ii Ctd; Multiple Sequence Alignment; Microarray Data; Protein; Expression; Ctd; Genes; Methylation; Elongation; Nucleosome; Reveals
ISSN (print) / ISBN 1097-2765
e-ISSN 1097-4164
Zeitschrift Molecular Cell
Quellenangaben Band: 73, Heft: 1, Seiten: 84-96 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Begutachtungsstatus Peer reviewed