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Ubiquitin-associated domain of Mex67 synchronizes recruitment of the mRNA export machinery with transcription.

ABSTRACT: The mRNA nuclear export receptor Mex67/Mtr2 is recruited to mRNAs through RNA-binding adaptors, including components of the THO/TREX complex that couple transcription to mRNA export. Here we show that the ubiquitin-associated (UBA) domain of Mex67 is not only required for proper nuclear export of mRNA but also contributes to recruitment of Mex67 to transcribing genes. Our results reveal that the UBA domain of Mex67 directly interacts with polyubiquitin chains and with Hpr1, a component of the THO/TREX complex, which is regulated by ubiquitylation in a transcription-dependent manner. This interaction transiently protects Hpr1 from ubiquitin/proteasome-mediated degradation and thereby coordinates recruitment of the mRNA export machinery with transcription and early messenger ribonucleoproteins assembly.

SUBMITTER: Gwizdek C 

PROVIDER: S-EPMC1637590 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature

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Ubiquitin-associated domain of Mex67 synchronizes recruitment of the mRNA export machinery with transcription.

Gwizdek Carole C   Iglesias Nahid N   Rodriguez Manuel S MS   Ossareh-Nazari Batool B   Hobeika Maria M   Divita Gilles G   Stutz Françoise F   Dargemont Catherine C  

Proceedings of the National Academy of Sciences of the United States of America 20061020 44

The mRNA nuclear export receptor Mex67/Mtr2 is recruited to mRNAs through RNA-binding adaptors, including components of the THO/TREX complex that couple transcription to mRNA export. Here we show that the ubiquitin-associated (UBA) domain of Mex67 is not only required for proper nuclear export of mRNA but also contributes to recruitment of Mex67 to transcribing genes. Our results reveal that the UBA domain of Mex67 directly interacts with polyubiquitin chains and with Hpr1, a component of the TH  ...[more]

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