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Nuclear mRNA quality control is bypassed for rapid export of stress responsive transcripts (Microarray)

ABSTRACT: Comparative analyses of Mex67 and Npl3 binding to mRNA at normal growth condition (25°C) and upon shift to heat stress (30 min, 42°C).

ORGANISM(S): Saccharomyces cerevisiae Schizosaccharomyces pombe

PROVIDER: GSE83267 | GEO | 2016/06/14

SECONDARY ACCESSION(S): PRJNA325561

REPOSITORIES: GEO

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Nuclear mRNA quality control is bypassed for rapid export of stress responsive transcripts [RNA-Seq]

Project description:Comparative analyses of Mex67 and Npl3 binding to mRNA at normal growth condition (25°C) and upon shift to heat stress (30 min, 42°C).

2016-12-13 | GSE81542 | GEO

Nuclear mRNA quality control is bypassed for rapid export of stress responsive transcripts (Microarray)

Project description:Comparative analyses of Mex67 and Npl3 binding to mRNA at normal growth condition (25Â°C) and upon shift to heat stress (30 min, 42Â°C). Comparative analyses of mRNA binding of Mex67, Npl3 and no tag control at normal growth condition (25Â°C) and upon heat stress (30 min, 42Â°C) via RNA Co-IP experiments. Respective co-purified mRNAs were subjected to cDNA Microarray chips.

2016-06-14 | E-GEOD-83267 | biostudies-arrayexpress

The shuttling SR-like proteins Gbp2 and Hrb1 mediate the nuclear export of spliced mRNAs

Project description:Three shuttling SR-like proteins exist in Saccharomyces cerevisiae, Npl3, Gbp2 and Hrb1, that are involved in the nuclear export of mRNAs. In a screen for genes that regulate the export of Gbp2, we identified novel mutants of the splicing factors PRP8 and PRP17 that lead to severe mislocalization defects for Gbp2 and Hrb1, but not Npl3. Microarray and qRT-PCR analyses show that Gbp2 and Hrb1 preferentially bind to transcripts derived from intron-containing genes. Moreover, in contrast to Npl3, Gbp2 and Hrb1 show genetic and physical interactions with late splicing factors such as Prp17 and Prp43. Further, RNA co-immunoprecipitation experiments reveal that, unlike Npl3, association of Gbp2 and Hrb1 with the mRNA requires splicing, and this in turn is required for their Mex67 recruitment. We propose a model in which Gbp2 and Hrb1 are attached to the mRNAs at late stages of splicing to promote the subsequent export of spliced mRNAs. keyword: RIP-chip RNA-IP of endogenously expressed 3-fold C-terminal myc-tagged Gbp2 and Hrb1 in S288C background cells was each performed once in cells grown to a density of 4x10^7 cells/ml and hybridized against a total (input) RNA reference.

2013-08-30 | E-GEOD-20738 | biostudies-arrayexpress

Quality control of spliced mRNAs requires the shuttling SR-proteins Gbp2 and Hrb1

Project description:Eukaryotic cells have to prevent the export of unspliced pre-mRNAs until intron removal is completed to avoid the expression of aberrant and potentially harmful proteins. Only mature RNAs associate with the export receptor Mex67 (mammalian TAP) and enter the cytoplasm. The underlying nuclear quality control mechanisms are still unclear. Here we show that two shuttling SR-proteins Gbp2 and Hrb1 are key surveillance factors for the selective export of spliced mRNAs in yeast. Their absence leads to the significant leakage of unspliced pre-mRNAs into the cytoplasm. They bind to pre-mRNAs and the spliceosome during splicing, where they are necessary for the surveillance of splicing and the stable binding of the TRAMP-complex to the spliceosome-bound transcripts. Faulty transcripts are marked for their degradation at the nuclear exosome. On correct mRNAs the SR-proteins recruit Mex67 upon completion of splicing to allow a quality controlled nuclear export. Altogether, these data identify a role for shuttling SR-proteins in mRNA surveillance and nuclear mRNA quality control. 6 samples, i.e. 2 replicates per protein Gbp2, Hrb1 and Npl3

2013-12-04 | E-GEOD-52808 | biostudies-arrayexpress

Splicing defects in RNA export receptor mutants

Project description:Comparison of splicing defects in Wild type and xpo1-1 mex67-5

2018-01-01 | GSE93307 | GEO

The SR-like protein Npl3 transfers mRNP components from the transcription site onto the mRNA

Project description:In order to determine specifically the RNA-binding function of proteins involved in nuclear mRNP assembly, we first determined the amino acids involved in RNA-binding by RNPXL. We identified about 100 amino acids cross-linked to RNA in vivo in the nuclear mRNP components Npl3, Nab2, Tho1, Mex67-Mtr2 and the TREX complex. Second, we can now specifically elucidate the function of the RNA-binding activity of these proteins by mutation of the identified amino acids. Npl3 is an SR-like protein with functions in transcription elongation, splicing, 3’ end processing, mRNP assembly and nuclear mRNA export. The middle part of Npl3 consists of two RNA recognition motif (RRM) domains, RRM1 and RRM2, connected by an eight amino acid long flexible linker. In order to analyze the function of the RNA-binding activity of Npl3, we mutated several amino acids that cross-linked to RNA. We generated three npl3 mutants, one in the RRM1, one in the linker and a third in the RRM2 domain, and elucidated the functional consequences of these mutations. Interestingly, these three npl3 mutants show different phenotypes. Thus, abrogation of mRNA-binding in different regions of Npl3 has different functional outcomes. Furthermore, analysis of the npl3-Linker mutant revealed a novel function of Npl3. Npl3 functions in the transfer of nuclear mRNP components from the site of transcription onto the mRNA. Taken together, we identify the in vivo RNA-binding sites of nuclear mRNA-binding proteins involved in mRNP assembly and nuclear mRNA export. In addition, we show that abrogation of RNA-binding in different regions of the protein Npl3 has specific and surprisingly different functional consequences. Furthermore, we uncovered a novel function of Npl3 in nuclear mRNP assembly.

2022-11-26 | GSE160709 | GEO

Genomic Run On (GRO): determination of the nascent transcriptional rates in a series of a mex67 mutant.

Project description:The goal of the project was to check the effect on transcription rate of a sudden depletion of Mex67 protein by using a thermosensitive mutant: mex67-5 Cells were grown in YPD at 26ÂºC to 0.5 OD600. At that time cells were shifted to 37ÂºC to induce Mex67 protein inactivation and recovered after, 0, 5, 20, 40, 60 and 150 min.

2015-12-31 | E-GEOD-65228 | biostudies-arrayexpress

Identification of genes responsive to hyperthermia in human leukemia U937 cells

Project description:Hyperthermia (41˚C <) is widely used to treat patients with various cancers. Here, the effects of hyperthermia (42˚C for 90 min) on the gene expression in human lymphoma U937 cells were investigated using an Affymetrix GeneChip system. The cells were treated with hyperthermia (42°C for 90 min) and followed by incubation for 0, 1, 3 or 6 h at 37°C. The percentage of DNA fragmentation was 7.5 ± 0.9 (mean ± SD), 10.1 ± 0.2, and 17.3 ± 2.3 at the incubation periods of 1, 3, and 6 h, respectively. Of approximately 47,000 probe sets analyzed, the hyperthermia down-regulated 4,214 probe sets and up-regulated 1,334 by a factor 2.0 or greater.

2008-11-11 | GSE13503 | GEO

RIP-seq analysis of Isw1 interacting transcripts

Project description:This experiment captures the poly(A)RNAs co-immunoprecipated with Isw1 in WT and npl3-1 cells. Chromatin remodelers play an essential role in regulating DNA transaction processes. The yeast chromatin remodeling complex ISW1 displays an unexpected function in nuclear mRNP surveillance, retaining premature mRNPs in proximity to their transcription site. This activity of ISW1 requires its recruitment onto chromatin, its interaction with mRNPs but not its nucleosome sliding activity. In npl3-1 cells, mRNA export is compromised resulting in an increased association of mRNAs with Isw1.

2016-11-17 | E-MTAB-4826 | biostudies-arrayexpress

Double stranded RNA formation leads to preferential nuclear export and gene expression

Project description:mRNAs are transcribed and processed in the nucleus before they are exported into the cytoplasm for translation. Export is mediated by the export receptor heterodimer Mex67-Mtr2 in yeast (TAP-p15 in humans). Interestingly, also many lncRNAs leave the nucleus but it is currently unclear why they travel into the cytoplasm. Here we show that antisense (as)RNAs accelerate mRNA export by annealing with their sense counterparts through the helicase Dbp2. These double-stranded (ds)RNAs dominate export compared to single-stranded (ss)RNA, as they have a higher capacity and affinity for the export receptor Mex67. In this way, asRNAs boost gene expression, which is beneficial for cells. This is particularly important upon expression program changes. Consequently, the degradation or prevention of the formation of dsRNA is toxic for cells. This mechanism illuminates the general cellular occurrence of asRNAs and explains their nuclear export.

2024-04-30 | GSE252951 | GEO

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