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Author Notes:

CD:dargemont.catherine@ijm.univ-paris-diderot.fr, Tel: 0033157278032.

We would like to thank C. Moore, L. Minvielle-Sebastia, C. Guthrie for reagents and V. Oréal for his help.

We are most grateful to B. Palancade, F. Stutz, J. Weitzman and V. Géli for critical reading of the manuscript.

Subjects:

Research Funding:

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:

  • Science & Technology
  • Life Sciences & Biomedicine
  • Biochemistry & Molecular Biology
  • Cell Biology
  • MESSENGER-RNA EXPORT
  • SACCHAROMYCES-CEREVISIAE
  • NUCLEAR EXPORT
  • TRANSCRIPTION TERMINATION
  • POLYADENYLATION FACTOR
  • YEAST
  • METHYLATION
  • COMPLEX
  • BINDING
  • MEX67P

H2B Ubiquitylation Controls the Formation of Export-Competent mRNP

Tools:

Journal Title:

Molecular Cell

Volume:

Volume 45, Number 1

Publisher:

, Pages 132-139

Type of Work:

Article | Post-print: After Peer Review

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.

Copyright information:

© 2012 Elsevier Inc. All rights reserved.

This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Creative Commons License

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