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Study of the cellular component-dependent functions of Xrn1

ABSTRACT: Study of the cellular component-dependent functions of Xrn1

PROVIDER: PRJNA798697 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17662522_1.fastq.gz	Fastqsanger.gz
	SRR17662522_2.fastq.gz	Fastqsanger.gz
	SRR17662523_1.fastq.gz	Fastqsanger.gz
	SRR17662523_2.fastq.gz	Fastqsanger.gz
	SRR17662524_1.fastq.gz	Fastqsanger.gz

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Study of the cellular component-dependent functions of Xrn1

Project description:The main cytoplasmic mRNA decay pathway in yeast uses the 5’-3’ exonuclease Xrn1 (Parker and Song, Nat Struct Mol Biol. 2004 ). This protein shuttles from the cytoplasm to the nucleus, where it has a role as transcription factor (Haimovich et al. Cell 2013). In this work, we find that most of the global phenotypes of an xrn1 mutant are partially complemented by a cytoplasmic version of the paralogous 5’-3’exonuclease Rat1 (cRat1) indicating that this 5’-3’-exonuclease has a similar enzymatic capacity as Xrn1. The lack of a cytoplasmatic 5’-3’-exoribonuclease is the cause of the physiological defects of an xrn1 mutant. The capacity of cRat1 to perform co-translational decay is, however, very limited. The comparison with the strain having a NLS1∆-NLS2∆-Xrn1 version shows that it is slightly deficient in 5’→3’-co-translational decay but much more efficient than cRat1. In both strains, cRat1 and -Xrn1-NLS1&2, the lack of nuclear Xrn1 has a very minor influence on cell growth.

2024-10-23 | GSE193992 | GEO

Transcription profiling of yeast wild type, xrn1, xrn1 upf1, xrn1 nmd2, and xrn1 upf3 strains to investigate mRNA decay

Project description:To determine the effects of inactivation of both the nosense-mediated mRNA decay pathway and the general 5' to 3' decay pathway on yeast mRNA decay, we compared the expression profiles of the wild-type, xrn1, xrn1 upf1, xrn1 nmd2, and xrn1 upf3 strains.

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XRN1 deletion induces PKR-dependent cell lethality in interferon-activated cancer cells

Project description:Emerging data suggest that induction of viral mimicry responses through activation of double-stranded RNA (dsRNA) sensors in cancer cells is a promising therapeutic strategy. One approach to induce viral mimicry is to target molecular regulators of dsRNA sensing pathways. Here, we show that the exoribonuclease XRN1 is a negative regulator of the dsRNA sensor protein kinase R (PKR) in cancer cells with high interferon-stimulated gene (ISG) expression. XRN1 deletion causes PKR pathway activation and consequent cancer cell lethality. Disruption of interferon signaling with the JAK1/2 inhibitor ruxolitinib can decrease cellular PKR levels and rescue sensitivity to XRN1 deletion. Conversely, interferon-b stimulation can increase PKR levels and induce sensitivity to XRN1 inactivation. Lastly, XRN1 deletion causes accumulation of endogenous complementary sense/anti-sense RNAs, which may represent candidate PKR ligands. Our data demonstrate how XRN1 regulates PKR, and how this interaction creates a vulnerability in cancer cells with an activated interferon cell state.

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Project description:RNA homeostasis, a process maintained through a balance between transcription and decay, plays a critical role for most cellular functions. The conserved XRN and DIS3 families are major exoribucleases involved in this RNA turnover. Very little information is currently available about their physiological and physiopathological functions in humans. The aim of this study was to identify the possible advantage and the subsequent modification changes associated with XRN1 invalidation (siXRN1).

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Project description:mRNA degradation is one of the main steps of gene expression, and a key player is the 5’-3’ exonuclease Xrn1. In Saccharomyces cerevisiae, it was previously shown, by a microscopy approach, that Xrn1 is located to different cellular compartments, depending on physiological state. During exponential growth, Xrn1 is distributed in the cytoplasm, while it is present in the eisosomes after the post-diauxic shift (PDS). Here, we biochemically characterized the Xrn1-associated complexes in different cellular states. We demonstrate that, after PDS, Xrn1 but not the decapping (DCP), nor Lsm1-7/Pat1 complexes, was sequestered in the eisosomes, thus preserving mRNAs from degradation.

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Xrn1 biochemically associates to the eisosome after the post diauxic shift in yeast (2)

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Xrn1 biochemically associates to the eisosome after the post diauxic shift in yeast (4)

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Xrn1 biochemically associates to the eisosome after the post diauxic shift in yeast (3)

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Project description:Antisense (as)lncRNAs are extensively degraded by the nuclear exosome and the cytoplasmic exoribonuclease Xrn1 in the budding yeast Saccharomyces cerevisiae, lacking RNA interference (RNAi). Whether the ribonuclease III Dicer affects aslncRNAs in close RNAi-capable relatives remains unknown. Using genome-wide RNA profiling, here we show that aslncRNAs are primarily targeted by the exosome and Xrn1 in the RNAi-capable budding yeast Naumovozyma castellii, Dicer only affecting Xrn1-sensitive lncRNAs (XUTs) levels in Xrn1-deficient cells. The dcr1 and xrn1 mutants display synergic growth defects, indicating that Dicer becomes critical in absence of Xrn1. Small RNA sequencing showed that Dicer processes aslncRNAs into small RNAs, with a preference for asXUTs. Consistently, Dicer localizes into the cytoplasm. Finally, we observed an expansion of the exosome-sensitive antisense transcriptome in N. castellii compared to S. cerevisiae, suggesting that the presence of cytoplasmic RNAi has reinforced the nuclear RNA surveillance machinery to temper aslncRNAs expression. Our data provide fundamental insights into aslncRNAs metabolism and open perspectives into the possible evolutionary contribution of RNAi in shaping the aslncRNAs transcriptome.

2019-08-21 | GSE90041 | GEO

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