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Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex

ABSTRACT: The S. pombe orthologue of the human PAXT complex, Mtl1-Red1 Core (MTREC), is an eleven-subunit complex which targets cryptic unstable transcripts (CUTs) to the nuclear RNA exosome for degradation. It encompasses the canonical poly(A) polymerase Pla1, responsible for polyadenylation of nascent RNA transcripts as part of the cleavage and polyadenylation factor (CPF/CPSF). In this study we identified and characterised the interaction between Pla1 and the MTREC complex core component Red1 and analysed the functional relevance of this interaction in vivo. Our crystal structure of the Pla1-Red1 complex showed that a 58-residue fragment in Red1 binds to the RNA recognition motif domain of Pla1 and tethers it to the MTREC complex. Structure-based Pla1-Red1 interaction mutations showed that Pla1, as part of MTREC complex, hyper-adenylates CUTs for their efficient degradation. Interestingly, the Red1-Pla1 interaction was also required for the efficient assembly of the fission yeast facultative heterochromatic islands. Together, our data suggest a complex interplay between the RNA surveillance and 3â€™-end processing machineries.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Fungi Schizosaccharomyces Pombe Spk1820

SUBMITTER: Frank Stein

LAB HEAD: Tamas Fischer

PROVIDER: PXD035413 | Pride | 2022-12-01

REPOSITORIES: Pride

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			Action	DRS
	F100543.dat	Other
	Lara_200924_P1314_PH_SK_adjusted_R1.raw	Raw
	P1314_PH_SK_adjusted_Lara_200924_P1314_PH_SK_adjusted_R1_results_20201217_1328_peptides.txt	Txt
	P1314_PH_SK_adjusted_Lara_200924_P1314_PH_SK_adjusted_R1_results_20201217_1328_proteins.txt	Txt
	P1314_PH_SK_adjusted_Lara_200924_P1314_PH_SK_adjusted_R1_results_20201217_1328_summary.txt	Txt

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