H2B Ubiquitylation Controls the Formation of Export-Competent mRNP

• Type of Material: Article
• Authors: Adeline Vitaliano-Prunier, University of Paris Diderot; Anna Babour, University of Paris Diderot; Lucas Herissant, University of Paris Diderot; Luciano Apponi, Emory University; Thanasis Margaritis, University Medical Center Utrecht; Frank C.P. Holstege, University Medical Center Utrecht; Anita Corbett, Emory University; Carole Gwizdek, University of Paris Diderot; Catherine Dargemont, University of Paris Diderot
• Language: English
• Date: 2012-01-13
• Publisher: Elsevier (Cell Press): 12 month embargo
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: © 2012 Elsevier Inc. All rights reserved.
• License: Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1016/j.molcel.2011.12.011
• Title of Journal or Parent Work: Molecular Cell
• ISSN: 1097-2765
• Volume: 45
• Issue: 1
• Start Page: 132
• End Page: 139
• Grant/Funding Information: This study was funded by grants from the Agence Nationale pour la Recherche (BLAN1227-01 to CD); and the Ligue contre le Cancer (CD’s team is “Equipe labellisee”).; LH is supported by the University Paris V; AVP by the Agence Nationale pour la Recherche; and AB by the Association de Recherche contre le Cancer.
• Keywords: COMPLEX; Biochemistry & Molecular Biology; Science & Technology; MESSENGER-RNA EXPORT; METHYLATION; YEAST; POLYADENYLATION FACTOR; NUCLEAR EXPORT; SACCHAROMYCES-CEREVISIAE; Life Sciences & Biomedicine; TRANSCRIPTION TERMINATION; MEX67P; Cell Biology; BINDING
• Research Categories: Chemistry, Biochemistry; Biology, Molecular

Abstract

Histone H2B ubiquitylation is a transcription-dependent modification that not only regulates nucleosome dynamics but also controls the trimethylation of histone H3 on lysine 4 by promoting ubiquitylation of Swd2, a component of both the histone methyltransferase COMPASS complex and the cleavage and polyadenylation factor(CPF). We show that preventing either H2B ubiquitylation or H2B-dependent modification of Swd2 results in nuclear accumulation of poly(A) RNA due to a defect in the integrity and stability of APT, a subcomplex of the CPF. Ubiquitin-regulated APT complex dynamics is required for the correct recruitment of the mRNA export receptor Mex67 to nuclear mRNPs. While H2B ubiquitylation controls the recruitment of the different Mex67 adaptors to mRNPs, the effect of Swd2 ubiquitylation is restricted to Yra1 and Nab2, which, in turn, controls poly(A) tail length. Modification of H2B thus participates in the crosstalk between cotranscriptional events and assembly of mRNPs linking nuclear processing and mRNA export.