Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cdk11-Cyclin L controls the assembly of the RNA polymerase II Mediator

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Schizosaccharomyces pombe

PROVIDER: GSE37962 | GEO | 2014/07/11

SECONDARY ACCESSION(S): PRJNA165837

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Cdk11-Cyclin L controls the assembly of the RNA polymerase II Mediator

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2014-07-11 | E-GEOD-37962 | biostudies-arrayexpress

Cdk11-Cyclin L controls the assembly of the RNA polymerase II Mediator [expression]

Project description:The L-Mediator is a general co-activator of RNA Polymerase II transcription and is formed by the reversible association of the S-Mediator and the kinase module harbouring Cdk8. We describe the Cdk11-Lcp1 complex and show that its inactivation alter the global expression profiles in a very similar way than mutations of the kinase module. Cdk11 is broadly distributed onto chromatin and phosphorylate the Med27 and Med4 Mediator subunits on conserved residues. The inactivation of either Cdk11 or the mutation of its target residues on the Mediator leads to a strongly decreased association of the kinase module and the S-Mediator. The results show that Cdk11-Lcp1 regulates that assembly of the L-Mediator complex. Total RNA was isolated from two biological replicates for all conditions, and each biological replicate was hybridized in duplicate on Agilent arrays (dye-swap).

2014-07-11 | E-GEOD-37960 | biostudies-arrayexpress

Cdk11-Cyclin L controls the assembly of the RNA polymerase II Mediator [expression]

2014-07-11 | GSE37960 | GEO

Cdk11-Cyclin L controls the assembly of the RNA polymerase II Mediator [ChIP-chip]

Project description:The L-Mediator is a general co-activator of RNA Polymerase II transcription and is formed by the reversible association of the S-Mediator and the kinase module harbouring Cdk8. We describe the Cdk11-Lcp1 complex and show that its inactivation alter the global expression profiles in a very similar way than mutations of the kinase module. Cdk11 is broadly distributed onto chromatin and phosphorylate the Med27 and Med4 Mediator subunits on conserved residues. The inactivation of either Cdk11 or the mutation of its target residues on the Mediator leads to a strongly decreased association of the kinase module and the S-Mediator. The results show that Cdk11-Lcp1 regulates that assembly of the L-Mediator complex. Two independent immunoprecipitations were done for HA-tagged Cdk11 and each biological replicate was hybridized in duplicate on Agilent arrays using input DNA as the reference channel.

2014-07-11 | E-GEOD-37961 | biostudies-arrayexpress

Cdk11-Cyclin L controls the assembly of the RNA polymerase II Mediator [ChIP-chip]

2014-07-11 | GSE37961 | GEO

Condensin Controls Recruitment of RNA Polymerase II to Achieve X-Chromosome Dosage Compensation

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2013-06-18 | E-GEOD-43087 | biostudies-arrayexpress

Tat controls RNA Polymerase II and the epigenetic landscape to precisely rewire cellular transcriptional programs

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2015-06-15 | E-GEOD-65689 | biostudies-arrayexpress

Activator-mediator binding stabilizes RNA polymerase II orientation within the human mediator-RNA polymerase II-TFIIF assembly.

Project description:The human Mediator complex controls RNA polymerase II (pol II) function in ways that remain incompletely understood. Activator-Mediator binding alters Mediator structure, and these activator-induced structural shifts appear to play key roles in regulating transcription. A recent cryo-electron microscopy (EM) analysis revealed that pol II adopted a stable orientation within a Mediator-pol II-TFIIF assembly in which Mediator was bound to the activation domain of viral protein 16 (VP16). Whereas TFIIF was shown to be important for orienting pol II within this assembly, the potential role of the activator was not assessed. To determine how activator binding might affect pol II orientation, we isolated human Mediator-pol II-TFIIF complexes in which Mediator was not bound to an activator. Cryo-EM analysis of this assembly, coupled with pol II crystal structure docking, revealed that pol II binds Mediator at the same general location; however, in contrast to VP16-bound Mediator, pol II does not appear to stably orient in the absence of an activator. Variability in pol II orientation might be important mechanistically, perhaps to enable sense and antisense transcription at human promoters. Because Mediator interacts extensively with pol II, these results suggest that Mediator structural shifts induced by activator binding help stably orient pol II prior to transcription initiation.

| S-EPMC4582759 | biostudies-literature

RNA polymerase II collision interrupts convergent transcription

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2012-11-30 | E-GEOD-38384 | biostudies-arrayexpress

Arginine citrullination at the C-terminal domain controls RNA Polymerase II transcription

Project description:This SuperSeries is composed of the SubSeries listed below.

2018-11-21 | GSE105795 | GEO