Journal Article

Sumoylation of the THO complex regulates the biogenesis of a subset of mRNPs

Hugo Bretes, Jérôme O. Rouviere, Thibaut Leger, Marlene Oeffinger, Frédéric Devaux, Valérie Doye and Benoit Palancade

in Nucleic Acids Research

Volume 42, issue 8, pages 5043-5058
Published in print April 2014 | ISSN: 0305-1048
Published online February 2014 | e-ISSN: 1362-4962 | DOI: http://dx.doi.org/10.1093/nar/gku124

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Assembly of messenger ribonucleoparticles (mRNPs) is a pivotal step in gene expression, but only a few molecular mechanisms contributing to its regulation have been described. Here, through a comprehensive proteomic survey of mRNP assembly, we demonstrate that the SUMO pathway specifically controls the association of the THO complex with mRNPs. We further show that the THO complex, a key player in the interplay between gene expression, mRNA export and genetic stability, is sumoylated on its Hpr1 subunit and that this modification regulates its association with mRNPs. Altered recruitment of the THO complex onto mRNPs in sumoylation-defective mutants does not affect bulk mRNA export or genetic stability, but impairs the expression of acidic stress-induced genes and, consistently, compromises viability in acidic stress conditions. Importantly, inactivation of the nuclear exosome suppresses the phenotypes of the hpr1 non-sumoylatable mutant, showing that SUMO-dependent mRNP assembly is critical to allow a specific subset of mRNPs to escape degradation. This article thus provides the first example of a SUMO-dependent mRNP-assembly event allowing a refined tuning of gene expression, in particular under specific stress conditions.

Journal Article.  8930 words.  Illustrated.

Subjects: Chemistry ; Biochemistry ; Bioinformatics and Computational Biology ; Genetics and Genomics ; Molecular and Cell Biology

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