Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

ABSTRACT: 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).

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Alexander Leitner

LAB HEAD: Alexander Leitner

PROVIDER: PXD019751 | Pride | 2021-02-04

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Sigma3_file_overview.xlsx	Xlsx
	TRiCs3_closed_R1.xlsx	Xlsx
	TRiCs3_closed_R2.xlsx	Xlsx
	TRiCs3_open_R1.xlsx	Xlsx
	TRiCs3_open_R2.xlsx	Xlsx

Items per page:

1 - 5 of 30

Similar Datasets

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

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

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

A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT

Project description:Chemical cross-linking coupled to mass spectrometry was used to study assembly intermediates of the chaperonin TRiC/CCT. Complex were cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2023-08-24 | PXD043532 | 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

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

A precisely positioned MED12 activation helix stimulates CDK8 kinase activity

Project description: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.

2020-01-16 | PXD015394 | 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

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

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