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RNA-seq analysis in WT and rpb1-CTD-S2A strains

ABSTRACT: RNA-seq analysis in WT and rpb1-CTD-S2A strains

PROVIDER: PRJNA719083 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14128934_1.fastq.gz	Fastqsanger.gz
	SRR14128934_2.fastq.gz	Fastqsanger.gz
	SRR14128935_1.fastq.gz	Fastqsanger.gz
	SRR14128935_2.fastq.gz	Fastqsanger.gz
	SRR14128936_1.fastq.gz	Fastqsanger.gz

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RNA-seq analysis in WT and rpb1-CTD-S2A strains

Project description:We report calibrated transcriptome of rpb1-CTD-S2A and WT of S. pombe cells. Phosphorylation of the RNA polymerase II (Pol II) C-terminal domain on heptad Y1S2P3T4S5P6S7 coordinates key events during transcription and when its deregulation leads to defects in transcription and RNA processing. Here we report that alanine substitution of all Ser2 in CTD result in increased antisense transcription.

2021-08-26 | GSE171307 | GEO

Modification of C-terminal Domain (CTD) of RPB1 plays a role in transcriptome change upon salt stress

Project description:Transctriptome profiling of CTD-14 repeats, 2A, 5A mutants responding to 0.7N NaCl for 30mins. The study shows that phosphorylation at Ser5 sites plays a role in normal induction and repression of genes upon NaCl stress. The CTD14 strains harbors a plasmid expressing RPB1 with 14 wild-type CTD repeats. 5A strains carries a plasmid expressing a chimeric RPB1 in which the CTD was composed of 5 repeats of CTD-serine 5 substituted with Ala followed by 7 wild-type-sequenced repeats. The 2A strains carrys 8 repeats of CTD-serine 2 substituted with alanine followed by 7 wild-type-sequenced repeats.

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Modification of C-terminal Domain (CTD) of RPB1 plays a role in transcriptome change upon salt stress

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Expression profiling of rpb1-12XWTCTD and rpb1-12XS2ACTD fission yeast strains.

Project description:In fission yeast, the nuclear-localized Lsk1p-Lsc1p-Lsg1p cyclin dependent kinase complex is required for the reliable execution of cytokinesis and is also required for Ser-2 phosphorylation RNA pol II carboxy terminal domain. To address whether alterations in CTD phosphorylation might selectively alter expression of cytokinesis genes, expression profiling of site-directed CTD mutants was performed. Strains bearing the rpb1-12XCTD and rpb1-12XS2ACTD mutations were grown to mid-log phase in YES media and treated with 0.5uM LatA (or the solvent control, DMSO) for three hours at 30C. Three biological replicates were performed.

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The consequences of RPB1-CTD truncation for human transcriptome dynamics

Project description:The carboxy-terminal domain of RPB1 subunit of RNA Polymerase II (CTD) plays an essential function in the regulation of gene expression and the coordination of co-transcriptional processes. CTD consists of hepta-amino acid repeats varying in number from 52 in humans to 26 in yeast and its length is crucial for spatial organization of transcriptional machinery in the nucleus. We found that the proximal half of the CTD is sufficient to support RNA metabolism and co-transcriptional processing in steady state conditions in human cells. Signal induced transcription, however, is severely impaired upon CTD shortening. Our data suggest that CTD length increased in evolution to allow for spatio-temporal control of gene expression patterns at least in part by facilitating enhancer function.

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MudPIT analysis of proteins interacting with Saccharomyces cerevisiae RNA Polymerase II HA-Rpb1 C-Terminal Domain

Project description:The carboxy-terminal domain (CTD) of Rpb1, the largest component of the 12-subunit RNA polymerase II, consists of repeating Y1S2P3T4S5P6S7 heptapeptides (26 repeats in budding yeast). Each stage of transcription relies on the ordered recruitment and exchange of specific protein complexes that act on RNA polymerase II, its nascent transcripts, and the underlying chromatin. This dynamic process is orchestrated via patterned post-translational modifications of the CTD. To characterize the role of phosphorylation on Thr4, we examined the effect of Rpb1 alleles in which Thr4 was substituted with an alanine (T4A) or the phospho-mimic glutamate (T4E). Substitutions were made across all heptad repeats of the CTD. We affinity purified HA-tagged Rpb1 from Saccharomyces cerevisiae strains bearing WT, T4A, and T4E CTDs. A control strain (Z26) lacking the HA-tagged Rpb1 was subjected to an identical affinity enrichment procedure. Three biological replicates were acquired for each type of affinity purification and analyzed independently. After TCA-precipitation, proteins were urea-denatured, reduced, alkylated, then digested with endoproteinase LysC followed by trypsin. The resulting peptide mixtures were analyzed by Multidimensional Protein Identification Technology (MudPIT). Label-free quantitative proteomics was used to identify and quantify the relative abundance of affinity-enriched complexes.

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ChIp-on-chip with Rbp3 in C-ternimal domain (CTD) of Rbp1 mutants upon Nacl Stress in yeast

2014-12-03 | E-GEOD-60707 | biostudies-arrayexpress

The consequences of RPB1-CTD truncation for human transcriptome dynamics

Project description:The consequences of RPB1-CTD truncation for human transcriptome dynamics

| PRJNA667687 | ENA