TY - JOUR
T1 - H2B ubiquitylation controls the formation of export-competent mRNP
AU - Vitaliano-Prunier, Adeline
AU - Babour, Anna
AU - Hérissant, Lucas
AU - Apponi, Luciano
AU - Margaritis, Thanasis
AU - Holstege, Frank C.P.
AU - Corbett, Anita H.
AU - Gwizdek, Carole
AU - Dargemont, Catherine
N1 - Funding Information:
We would like to thank C. Moore, L. Minvielle-Sebastia, and 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. This study was funded by grants from the Agence Nationale pour la Recherche (BLAN1227-01 to C.D.) and the Ligue contre le Cancer (C.D.'s team is “Equipe labellisée”). L.H. is supported by the University Paris V; A.V.P. by the Agence Nationale pour la Recherche; and A.B. by the Association de Recherche contre le Cancer.
PY - 2012/1/13
Y1 - 2012/1/13
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84855864819&partnerID=8YFLogxK
U2 - 10.1016/j.molcel.2011.12.011
DO - 10.1016/j.molcel.2011.12.011
M3 - Article
C2 - 22244335
AN - SCOPUS:84855864819
SN - 1097-2765
VL - 45
SP - 132
EP - 139
JO - Molecular Cell
JF - Molecular Cell
IS - 1
ER -