Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cross-linking coupled with mass spectrometry (XL-MS) analysis of TRiC-PDCD5 complex

ABSTRACT: In order to investigate the interaction between TRiC and PDCD5 proteins, purified PDCD5 and TRiC were incubated for XL-MS analysis. A total of 1094 cross-linked peptides were identified.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Yueshuai Guo

LAB HEAD: Chen Pan

PROVIDER: PXD068864 | Pride | 2026-01-08

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Search.zip	Other
	checksum.txt	Txt
	congyao143-10s.raw	Raw
	congyao143-15s.raw	Raw
	congyao143-5s.raw	Raw

Items per page:

1 - 5 of 5

Similar Datasets

Proteomics analysis of TRiC interactome from Stra8-Pdcd5-/- mouse elongating spermatids

Project description:In order to investigate the interaction proteins of TRiC in Stra8-Pdcd5-/- elongating spermatids, TRiC immunoprecipitation from Pdcd5F/F and Stra8-Pdcd5-/- elongating spermatids were collected for LC-MS/MS analysis. A total of 4419 proteins were quantified, and 375 proteins (p < 0.05, Foldchange > 1.5) were differentially expressed. Among these differential proteins, 83 proteins were downregulated (22%) and 292 proteins were upregulated (78%) in Stra8-Pdcd5-/- elongating spermatids.

2026-01-08 | PXD067989 | Pride

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [RNA-seq]

Project description:The molecular chaperonin TRiC/CCT is a large hetero-oligomeric structure that serves an essential role in eukaryotic cells by minimally supporting protein homeostasis including the folding of nascent polypeptides and the assembly/disassembly of protein complexes. TRiC/CCT is typically considered a strict cytosolic machine. Here, we investigated the influence of TRiC/CCT on nuclear features including epigenetic marks, chromatin accessibility, and transcription. Despite being linked to several chromatin modifiers, our work indicates TRiC/CCT does not have a sustained role with these factors. TRiC/CCT did actively contribute to transcription. Inactivation of TRiC/CCT resulted in a significant increase in the production of RNA leading to an accumulation of noncoding transcripts. Our data support a direct role for TRiC/CCT with RNA polymerase II as the chaperonin modulated nascent RNA production both in vivo and in vitro. Overall, our studies reveal a new avenue by which TRiC/CCT contributes to cell homeostasis by regulating the activity of nuclear RNA polymerase II.

2025-09-01 | GSE274453 | GEO

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [DNase-Seq]

2025-09-01 | GSE274455 | GEO

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [4tU-Seq]

2025-09-01 | GSE274454 | GEO

TRiC controls transcription resumption after UV damage by regulating Cockayne Syndrome protein A

Project description:Transcription-blocking DNA lesions are removed by transcription-coupled nucleotide excision repair (TC-NER) to preserve cell viability. TC-NER is triggered by the stalling of RNA polymerase II at DNA lesions, leading to the recruitment of TC-NER-specific factors such as the CSA-DDB1-CUL4A-RBX1 cullin-RING ubiquitin ligase complex (CRLCSA). Despite its vital role in TC-NER, little is known about the regulation of the CRLCSA complex during TC-NER. Using conventional and cross-linking immunoprecipitations coupled to mass spectrometry, we uncover a stable interaction between CSA and the TRiC chaperonin. TRiC’s binding to CSA ensures its stability and DDB1-dependent assembly into the CRLCSA complex. Consequently, loss of TRiC leads to mislocalization and depletion of CSA, as well as impaired transcription recovery following UV damage, suggesting defects in TC-NER. Furthermore, Cockayne syndrome (CS)-causing mutations in CSA lead to increased TRiC binding and a failure to compose the CRLCSA complex. Thus, we uncover CSA as a novel TRiC substrate and reveal a role for TRiC in regulating CSA-dependent TC-NER and the development of CS.

2018-05-02 | PXD008868 | Pride

Round or columnar and hypertrophic chondrocytes of Tric-b-KO mice

Project description:To survey altered gene expreesion in round, colmnar and hypertrophic chondrocytes of Tric-b-KO mice, total RNA preparations from round chondrocytes and colmnar/hypertrophic chondrocytes were subjected to gene microarray analysis. Results provide insight into the transcriptional profile of each Tric-b-KO chondrocyte and provide further insight into their functions.

2023-01-31 | GSE223776 | GEO

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

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

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

Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT

Project description:Folding newly synthesized proteins relies on the ribosome intricately coordinating mRNA translation with a network of ribosome-associated machinery. The principles that drive the coordination of this diverse machinery remain poorly understood. Here, we use selective ribosome profiling to determine how the essential chaperonin TRiC/CCT and the Hsp70 Ssb are recruited to ribosome-nascent chain complexes to mediate cotranslational protein folding. Whereas substrate localization and nascent chain sequence are the major determinants of cotranslational recruitment of Ssb, we found that temporal and structural elements drive TRiC engagement. For both chaperones, however, local slowdowns in translation enhance chaperone enrichment. This work helps define the principles that dictate the coordinated activity of ribosome-associated factors to perform their critical role in maintaining a properly folded nascent proteome.

2019-08-22 | GSE114882 | GEO