Clpxp - OmicsDI

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Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V. Otto-Hahn-Straße 6b 44227 Dortmund, Germany P: +49 (0)2 31.13 92-100 F: +49 (0)2 31.13 92-200 www.isas.de (1)
Stephan A. Sieber, Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, Garching b. München 85747, Germany; Chair of Organic Chemistry II, Technische Universität München, Garching b. München 85747, Germany (1)
Forschungszentrum Juelich GmbH ZEA-3 Analytics Wilhelm-Johnen-Str D-52425 Juelich Germany (1)

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Chemical cross-linking enables drafting ClpXP proximity maps and taking snapshots of in vivo interaction networks

Protein-protein interactions within complexes and networks are often dynamic and their elucidation remains a challenging task. Here, we show on the example of the proteolytic ClpXP complex the power of combined chemical cross-linking and mass-spectrometry to capture transient binding interactions wi...

ORGANISM(S): Homo sapiens (Human) Escherichia coli Staphylococcus aureus

2018-11-21 | PXD009224 | Pride

Identification of potential mitochondrial CLPXP protease interactors and substrates

Maintenance of mitochondria is achieved by several mechanisms, including the regulation of mitochondrial proteostasis. The matrix protease CLPXP, involved in protein quality control, has been implicated in ageing and disease. However, particularly due to the lack of knowledge of CLPXP’s substrate sp...

ORGANISM(S): Podospora

2016-07-27 | PXD003264 | Pride

Mitochondria Aging Clpxp protease

Proteome-wide identification of in vitro substrates for P. aeruginosa ClpXP

we treated the cell lysates of ΔclpX mutant with or without P. aeruginosa ClpXP protease and used Label-free quantitative techniques (LFQ) to identify and quantify the proteolytic targets of ClpXP (p.aeruginosa PAO1). As a result, 3338 proteins were identified and 2493 proteins were quantified. The ...

ORGANISM(S): Pseudomonas aeruginosa PAO1

2020-04-29 | PXD014928 | Pride

Proteolytic targets Label-free quantification lc-ms/ms P.aeruginosa pao1 Clpxp

Degradation of MinD oscillator complexes by Escherichia coli ClpXP.

Not available

S-EPMC7857489 | biostudies-literature

Inducible synthetic protein degradation system for phenotype control

Synthetic control of cell factory phenotypes is needed for redirecting resources from cell growth to production. To achieve that ClpXP proteasome was introduced to yeast Saccharomyces cerevisiae under control of TetON induction. Growth essential (in synthetic defined medium) metabolic enzymes Acc1, ...

ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast)

2023-05-10 | PXD034451 | Pride

Saccharomyces cerevisiae Clpxp proteasome

Serine phosphorylation facilitates protein degradation by the human mitochondrial ClpXP protease.

Not available

S-EPMC11804671 | biostudies-literature

ClpXP degrades SsrA-tagged proteins in Streptococcus pneumoniae.

Not available

S-EPMC2668424 | biostudies-literature

ClpXP, an ATP-powered unfolding and protein-degradation machine.

Not available

S-EPMC3209554 | biostudies-literature