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DEAD-box ATPase Dbp2 mediates mRNA release after 3’-end formation

ABSTRACT: mRNA biogenesis in the eukaryotic nucleus is a highly complex process. The numerous RNA processing steps are spatially and temporally coordinated to ensure that only fully processed transcripts are released into the nucleoplasm for export from the nucleus. Here, we explore the hypothesis that fission yeast Dbp2, a ribonucleoprotein complex (RNP) remodelling ATPase of the DEAD-box family, is involved in a RNP assembly checkpoint at the 3’-end of genes that is coupled to the release of the 3’-end processing complex after polyadenylation. We show that Dbp2 interacts with the cleavage and polyadenylation complex (CPAC) and localizes 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, which is accompanied by a depletion of CPAC components from the soluble pool. Under these conditions, cells display an increased likelihood to skip polyadenylation sites as well as delayed transcription termination, suggesting that the availability of CPAC components is insufficient to maintain normal levels of 3’-end processing. Our data is consistent with a model in which Dbp2 is involved in an mRNP remodelling checkpoint that licenses RNA export and is coupled to CPAC release.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Schizosaccharomyces Pombe 927

TISSUE(S): Cell Culture

SUBMITTER: Timo Glatter

LAB HEAD: Timo Glatter

PROVIDER: PXD048560 | Pride | 2024-07-04

REPOSITORIES: Pride

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			Action	DRS
	Dbp2-1-1.raw	Raw
	Dbp2-1-2.raw	Raw
	Dbp2-1-3.raw	Raw
	Dbp2-1-4.raw	Raw
	Dbp2-1-5.raw	Raw

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