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

ABSTRACT: Mechanistic insights into the role of the canonical poly(A) polymerase Pla1 in RNA surveillance by the fission yeast MTREC complex

PROVIDER: PRJNA849209 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR19654143_1.fastq.gz	Fastqsanger.gz
	SRR19654143_2.fastq.gz	Fastqsanger.gz
	SRR19654144_1.fastq.gz	Fastqsanger.gz
	SRR19654144_2.fastq.gz	Fastqsanger.gz
	SRR19654145_1.fastq.gz	Fastqsanger.gz

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

Project description: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.

2022-12-01 | PXD035413 | Pride

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

Project description:In this study we analysed the functional relevance of the interaction between Pla1 and the MTREC complex core component Red1 using various high throughput sequencing analyses performed on different Pla1-Red1 interaction mutants.Our analyses revealed that as part of MTREC complex, Pla1 hyper-adenylates Cryptic Unstable Transcripts (CUTs) for their efficient degradation. Interestingly, our H3K9(me)2 ChIP seq. data analysis also showed us that a functional 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 3’-end processing machineries.

2022-12-22 | GSE206106 | GEO

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The non-canonical poly(A) polymerase FAM46C promotes erythropoiesis [RNA-seq]

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The non-canonical poly(A) polymerase FAM46C promotes erythropoiesis [CUT&RUN]

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

Project description:The S. pombe orthologue of the human PAXT connection, Mtl1-Red1 Core (MTREC), is an eleven-subunit complex that 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 identify and characterise the interaction between Pla1 and the MTREC complex core component Red1 and analyse the functional relevance of this interaction in vivo. Our crystal structure of the Pla1-Red1 complex shows 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 show that Pla1, as part of MTREC complex, hyper-adenylates CUTs for their efficient degradation. Interestingly, the Red1-Pla1 interaction is 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 3'-end processing machineries.

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The fission yeast MTREC complex targets CUTs and unspliced mRNAs to the nuclear exosome [expression array]

Project description:Cryptic unstable transcripts (CUTs) are rapidly degraded by the nuclear exosome, however, the way they are recognized and targeted to the exosome is not fully understood. The recently identified Schizosaccharomyces pombe MTREC complex has been shown to promote degradation of meiotic mRNAs and regulatory ncRNAs. Here, we report that the MTREC complex is also the major nuclear exosome targeting complex for CUTs and unspliced mRNAs. MTREC complex specifically binds to CUTs, meiotic mRNAs and unspliced mRNA transcripts and targets these RNAs for degradation by the nuclear exosome, while the TRAMP complex has only a minor role in this process. The MTREC complex physically interacts with the nuclear exosome and with various RNA-binding and -processing complexes, coupling RNA processing to the RNA degradation machinery. Our study reveals the central role of the evolutionarily conserved MTREC complex in RNA quality control, and in the recognition and elimination of aberrant, cryptic transcripts. Genome-wide expression analysis of MTREC, Nuclear Exosome, TRAMP, Nrd complex members

2015-05-22 | GSE64979 | GEO

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