H2B ubiquitylation controls the formation of export-competent mRNP

Adeline Vitaliano-Prunier, Anna Babour, Lucas Hérissant, Luciano Apponi, Thanasis Margaritis, Frank C.P. Holstege, Anita H. Corbett, Carole Gwizdek, Catherine Dargemont

Research output: Contribution to journalArticlepeer-review

45 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)132-139
Number of pages8
JournalMolecular Cell
Volume45
Issue number1
DOIs
Publication statusPublished - 13 Jan 2012
Externally publishedYes

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