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Homo sapiens

ABSTRACT: The cohesin complex prevents Myc-induced replication stress

PROVIDER: PRJNA353350 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5015870_1.fastq.gz	Fastqsanger.gz
	SRR5015870_2.fastq.gz	Fastqsanger.gz
	SRR5015881_1.fastq.gz	Fastqsanger.gz
	SRR5015881_2.fastq.gz	Fastqsanger.gz
	SRR5015872_1.fastq.gz	Fastqsanger.gz

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The cohesin complex prevents Myc-induced replication stress

Project description:The cohesin complex is mutated in cancer and in a number of rare familiar syndromes collectively known as Cohesinopathies. In the latter case, cohesin deficiencies have been linked to transcriptional alterations affecting Myc and its target genes. Here, we set out to understand to what extent the role of cohesins in controlling cell cycle is dependent on Myc expression and activity. Inactivation of the cohesin complex by silencing the RAD21 subunit led to cell cycle arrest due to both transcriptional impairment of Myc target genes and alterations of replication forks, which were fewer and preferentially unidirectional. Ectopic activation of Myc in RAD21 depleted cells, fully rescued transcription and promoted S-phase entry but failed to sustain S-phase progression thus leading to a strong replicative stress response, which was associated to a robust DNA damage response, DNA damage checkpoint activation and synthetic lethality. Thus, the cohesin complex is dispensable for Myc dependent transcription but essential to prevent Myc induced replicative stress. This suggests the presence of a topological checkpoint orchestrated by cohesins that by regulating Myc level prevents S-phase entry and replicative stress in cohesion compromised cells.

2017-12-22 | GSE89799 | GEO

CDK12 prevents MYC-induced transcription-replication conflicts

Project description:CDK12 prevents MYC-induced transcription-replication conflicts

| PRJNA991561 | ENA

CDK12 prevents MYC-induced transcription-replication conflicts [BLISS]

Project description:CDK12 prevents MYC-induced transcription-replication conflicts [BLISS]

| PRJNA991555 | ENA

CDK12 prevents MYC-induced transcription-replication conflicts [RNA-seq]

Project description:CDK12 prevents MYC-induced transcription-replication conflicts [RNA-seq]

| PRJNA991550 | ENA

CDK12 prevents MYC-induced transcription-replication conflicts [EU-seq]

Project description:CDK12 prevents MYC-induced transcription-replication conflicts [EU-seq]

| PRJNA991554 | ENA

CDK12 prevents MYC-induced transcription-replication conflicts [EdU-seq]

Project description:CDK12 prevents MYC-induced transcription-replication conflicts [EdU-seq]

| PRJNA991567 | ENA

CDK12 prevents MYC-induced transcription-replication conflicts [ChIP-seq]

Project description:CDK12 prevents MYC-induced transcription-replication conflicts [ChIP-seq]

| PRJNA991553 | ENA

Crystal structure of Homo sapiens kynureninase.

Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.

| S-EPMC2531291 | biostudies-literature

Homo sapiens whole blood.

Project description:RNA extracted at 240min. Samples are rRNA depleted. Expression measurement of Homo sapiens genes.

2019-07-31 | GSE114179 | GEO

Cohesin-dependent chromosome loop extrusion is limited by transcription and stalled replication forks [ChIP-seq]

Project description:Genome function depends on regulated chromosome folding, and loop extrusion by the protein complex cohesin is essential for this multilayered organization. The chromosomal positioning of cohesin is controlled by transcription, and the complex also localizes to stalled replication forks. However, the role of transcription and replication in chromosome looping remains unclear. Here, we show that reduction of chromosome-bound RNA polymerase weakens normal cohesin loop extrusion boundaries, allowing cohesin to form new long-range chromosome cis interactions. Stress response genes activated by transcription inhibition are also shown to act as new loop extrusion boundaries. Furthermore, cohesin loop extrusion during early S-phase is jointly controlled by transcription and replication units. Together, the results reveal that replication and transcription machineries are chromosome folding regulators that block the progression of loop-extruding cohesin, opening for new perspectives on cohesin’s roles in genome function and stability.

2022-06-15 | GSE161522 | GEO

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