Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A precisely positioned MED12 activation helix stimulates CDK8 kinase activity

ABSTRACT: Chemical cross-linking coupled to mass spectrometry was used to study binary and ternary complexes involving cyclin-dependent kinase 8 (CDK8), cyclin-C, and subunit 12 of the Mediator complex (MED12). Cross-linking was performed using different cross-linking chemistries: (1) disuccinimidyl suberate (DSS); (2) a combination of pimelic acid dihydrazide (PDH) and the coupling reagent, DMTMM.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Alexander Leitner

LAB HEAD: Claus-D. Kuhn

PROVIDER: PXD015394 | Pride | 2020-01-16

REPOSITORIES: pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	MED12_file_overview.xlsx	Xlsx
	MED12_results_DSS.xlsx	Xlsx
	MED12_results_PDH_DMTMM.xlsx	Xlsx
	aleitner_D1710_049.raw	Raw
	aleitner_D1710_050.raw	Raw

Items per page:

1 - 5 of 91

Similar Datasets

Interactions of CDK19 with MED12 and cyclin-C assessed by chemical cross-linking mass spectrometry

Project description:Chemical cross-linking coupled to mass spectrometry was used to study binary and ternary complexes involving cyclin-dependent kinase 19 (CDK19), cyclin-C, and an N-terminal fragment of subunit 12 of the Mediator complex (MED12 1-100). Cross-linking was performed using disuccinimidyl suberate (DSS). These results were generated in the context of the study published as Klatt et al., A precisely positioned MED12 activation helix stimulates CDK8 kinase activity, Proc. Natl. Acad. Sci. USA 2020 (DOI: 10.1073/pnas.1917635117) with the associated data set PXD015394, but were not included in the article.

2020-05-18 | PXD019251 | Pride

The TRiC Chaperonin and Prefoldin Cooperate to Fold and Assemble Viral Capsid Oligomers

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the folding of the reovirus sigma3 protein by the chaperonin, TRiC/CCT. Cross-linking was performed using the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2021-02-04 | PXD019751 | Pride

Characterization of Integrator module INTS10-INTS13-INTS14 and its connection to the cleavage module Part I

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the complex between the Integrator complex subunits INTS13 (Asunder) and INTS14. Cross-linking was performed using disuccinimidyl suberate (DSS).

2020-06-18 | PXD015682 | Pride

Conformational coupling of redox-driven Na+ translocation in Vibrio cholerae NADH:quinone oxidoreductase

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the architecture of the NQR complex in absence and presence of the inhibitor DQA (2-decyl-4-quinazolinylamine). The complex was cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2023-08-31 | PXD039289 | Pride

Structural analysis of the native TREX complex from S. cerevisiae

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the endogenously purified S. cerevisiae TREX complex. Cross-linking was performed using (a) bis(sulfosuccinimidyl) suberate (BS3) or (b) a combination of adipic dihydrazide (ADH) and 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium (DMTMM) chloride.

2023-09-15 | PXD025843 | Pride

A structural mechanism for PP2A-B56alpha inhibition by CIP2A

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the structure of the oncoprotein CIP2A and its interaction with the B56alpha regulatory subunit of protein phosphatase 2A. Cross-linking was performed using disuccinimidyl suberate (DSS) or a combination of pimelic dihydrazide (PDH) and the coupling reagent DMTMM.

2022-10-21 | PXD020636 | Pride

Folding of beta-tubulin by the chaperonin TRiC/CCT studied by chemical cross-linking and mass spectrometry

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the folding of the client protein, beta-tubulin, by the chaperonin TRiC/CCT. Different complexes containing TRiC/CCT and/or the chaperone prefoldin were cross-linked in absence or presence of nucleotides with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2022-12-08 | PXD030590 | Pride

Characterization of Integrator module INTS10-INTS13-INTS14 and its connection to the cleavage module Part II

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the complex between the Integrator complex subunits INTS4, 9, 11, and a partial segment of INTS13 containing the C-terminal region (termed CMBM). Cross-linking was performed using disuccinimidyl suberate (DSS).

2020-06-18 | PXD017996 | Pride

Molecular architecture of the human tRNA ligase complex

Project description:Chemical cross-linking coupled to mass spectrometry was used to study two tRNA ligase complexes, one consisting of subunits RTCB, DDX1, CGI-99, FAM98B and Ashwin (“full tRLC”) and one lacking Ashwin (“core tRLC”). Cross-linking was performed using the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2021-12-15 | PXD025662 | Pride

Cross-linking mass spectrometry of a complex between the chaperonin TRiC/CCT and its cochaperones, prefoldin and phosducin-like protein 2A

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the architecture of the co-complex between TRiC/CCT, PFD and PhLP2A. The complex was cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2023-12-11 | PXD040144 | Pride