DEAD-box ATPase Dbp2 is the key enzyme in an mRNP assembly checkpoint at the 3’-end of genes and involved in the recycling of cleavage factors

Ebru Aydin, Silke Schreiner, Jacqueline Böhme, Birte Keil, Jan Weber, Bojan Žunar, Timo Glatter and Cornelia Kilchert ()
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Ebru Aydin: Justus-Liebig University Giessen
Silke Schreiner: Justus-Liebig University Giessen
Jacqueline Böhme: Justus-Liebig University Giessen
Birte Keil: Justus-Liebig University Giessen
Jan Weber: Justus-Liebig University Giessen
Bojan Žunar: University of Zagreb Faculty of Food Technology and Biotechnology
Timo Glatter: Max Planck Institute for Terrestrial Microbiology
Cornelia Kilchert: Justus-Liebig University Giessen

Nature Communications, 2024, vol. 15, issue 1, 1-20

Abstract: Abstract mRNA biogenesis in the eukaryotic nucleus is a highly complex process. The numerous RNA processing steps are tightly coordinated to ensure that only fully processed transcripts are released from chromatin for export from the nucleus. Here, we present the hypothesis that fission yeast Dbp2, a ribonucleoprotein complex (RNP) remodelling ATPase of the DEAD-box family, is the key enzyme in an RNP assembly checkpoint at the 3’-end of genes. We show that Dbp2 interacts with the cleavage and polyadenylation complex (CPAC) and localises to cleavage bodies, which are enriched for 3’-end processing factors and proteins involved in nuclear RNA surveillance. Upon loss of Dbp2, 3’-processed, polyadenylated RNAs accumulate on chromatin and in cleavage bodies, and CPAC components are depleted from the soluble pool. Under these conditions, cells display an increased likelihood to skip polyadenylation sites and a delayed transcription termination, suggesting that levels of free CPAC components are insufficient to maintain normal levels of 3’-end processing. Our data support a model in which Dbp2 is the active component of an mRNP remodelling checkpoint that licenses RNA export and is coupled to CPAC release.

Date: 2024
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DOI: 10.1038/s41467-024-51035-z

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