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Cross-Linking MS of Parvulin 14 and 17

ABSTRACT: Here we performed a set of cross linking experiments with Parvulin 14 and 17 in order to understand the intramolecular contacts the proteins form. Also we investigated the interaction of Par14 with actin using CL-MS.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Farnusch Kaschani

LAB HEAD: Farnusch Kaschani

PROVIDER: PXD053984 | Pride | 2025-08-25

REPOSITORIES: Pride

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			Action	DRS
	ACE_0366_AG01-C10.raw	Raw
	ACE_0366_AG01-C11.raw	Raw
	ACE_0366_AG01-C3.raw	Raw
	ACE_0366_AG01-C4.raw	Raw
	ACE_0366_AG01-C5.raw	Raw

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1 - 5 of 34

Publications

The Actin-Binding Prolyl-Isomerase Par17 Sustains Its Substrate Selectivity by Interdomain Allostery.

Sternberg Anna A Borger Jennifer Lynne JL Thies Mathilda M Matena Anja A Blueggel Mike M Kamba Bianca E BE Beuck Christine C Kaschani Farnusch F Kaiser Markus M Bayer Peter P

Proteins 20250312 9

The human peptidyl-prolyl-cis/trans isomerases (PPIases), Parvulin 14 and Parvulin 17, accelerate the cis/trans isomerization of Xaa-Pro moieties within protein sequences. By modulating the respective binding interfaces of their target proteins, they play a crucial role in determining the fate of their substrates within the cell. Although both enzymes share the same amino acid sequence, they have different cellular functions. This difference is due to a 25 residue N-terminal extension present in ...[more]

PMID: 40071814

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An UBX domain in UBXD1 organizes Ub binding at the C-terminus of the VCP/p97 AAA-ATPase

Project description:Identification of crosslinked peptides between UBXD1, Ubiquitin and p97 using different cross-linking approaches (chemical cross-linking with DSSO, photo crosslinking with incorporated BPA or photo-Met)

2023-05-25 | PXD039606 | Pride

An UBX domain in UBXD1 organizes Ub binding at the C-terminus of the VCP/p97 AAA-ATPase

Project description:Identification of crosslinked peptides between UBXD1 and HR23b using different cross-linking approaches (chemical cross-linking with DSSO and photo crosslinking with incorporated BPA).

2023-05-25 | PXD040984 | Pride

Normal respiratory chain capacity and physiology in mice with severely reduced levels of mitochondrial respirasomes; Cross-linking of intact mitochondria

Project description:The mammalian oxidative phosphorylation (OXPHOS) system in the inner mitochondrial membrane comprises respiratory chain complexes I-IV (CI-CIV) and ATP synthase. Together, these protein complexes harvest metabolic energy to generate ATP, the cellular energy currency. The inner mitochondrial membrane is abundant in OXPHOS complexes and CI, CIII and CIV exhibit specific protein-protein interactions to form stable supercomplex assemblies, exemplified by the respirasome (CI-CIII2-CIV). Respirasomes are conserved in evolution, and as well documented by biochemical and structural methods. However, their physiological roles are much debated, despite a substantial literature suggesting their importance in facilitating catalysis and regulating turnover in response to metabolic demand. To investigate the in vivo role of respirasomes, we deleted a short conserved, charged loop in the UQCRC1 subunit of CIII that contacts CI. The resulting homozygous knock-in mice show profoundly decreased levels of respirasomes on blue native polyacrylamide gel electrophoresis (BN-PAGE) and complexome profiling proteomics analyses of different tissues, although the individual complexes appear unaffected. In vivo The spatial organization of respirasomes in vivo was altered in knock-in mice as shown by cross-linking experiments on intact mitochondria. Surprisingly, the mutant mice are healthy, with normal respiratory chain capacity and normal exercise tolerance. Therefore, respirasomes are dispensable for OXPHOS function in vivo.

2023-03-11 | PXD031345 | Pride

Dynamic profiling of the protein life cycle in response to pathogens (protein)

Project description:Protein expression is regulated by production and degradation of mRNAs and proteins, but their specific relationships remain unknown. We combine measurements of protein production and degradation and mRNA dynamics to build a quantitative genomic model of the differential regulation of gene expression in LPS stimulated mouse dendritic cells. Changes in mRNA abundance play a dominant role in determining most dynamic fold changes in protein levels. Conversely, the preexisting proteome of proteins performing basic cellular functions is remodeled primarily through changes in protein production or degradation, accounting for over half of the absolute change in protein molecules in the cell. Thus, the proteome is regulated by transcriptional induction of novel cellular functions and remodeling of preexisting functions through the protein life cycle. Mouse primary dendritic cells were treated with LPS or mock stimulus and profiled over a 12-hour time course. Cells were grown in M-labeled SILAC media, which was replaced with H-labeled SILAC media at time 0. Aliquots were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, 9, and 12 hours post-stimulation and added to equal volumes of a master mix of unlabeled (L) cells for the purpose of normalization. RNA-Seq was performed at 0, 1, 2, 4, 6, 9, and 12 hours post-stimulation.

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Structure of Anabaena flos-aquae gas vesicles revealed by cryo-ET

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2023-03-30 | PXD038631 | Pride

An Optimized Miniaturized Filter Aided Sample Preparation Method for Sensitive Cross-linking Mass Spectrometry Analysis of Microscale Samples

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2025-01-03 | PXD051322 | Pride

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2025-07-21 | PXD052584 | Pride

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