Proteomics

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Acyldepsipeptide probes facilitate specific detection of caseinolytic protease P independent of its oligomeric and activity state


ABSTRACT: Caseinolytic protease P (ClpP) is a tetradecameric peptidase which assembles with chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) represent small molecule mimics of ClpX, which bind into hydrophobic pockets on the apical site of the complex and thereby induce activation of ClpP. Detection of ClpP has so far been facilitated with active site directed probes which depend on the activity and oligomeric state of the complex. In order to expand the scope of ClpP labeling, we here introduce a stepwise synthetic approach to customized ADEP photoprobes. Structure-activity relationship studies with small fragments and ADEP derivatives paired with modeling studies revealed design principles of suitable probe molecules. The derivatives were tested for activation of ClpP and subsequently applied in labeling studies of the wild type peptidase as well as enzymes bearing mutations at the active site and an oligomerization sensor. Satisfyingly, the ADEP photoprobes provided a labeling readout of ClpP independent of its activity and oligomeric state.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Staphylococcus Aureus

SUBMITTER: Barbara Hofbauer  

LAB HEAD: Stephan A. Sieber

PROVIDER: PXD015244 | Pride | 2020-05-26

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20190627_BBH245_266_01.raw Raw
20190627_BBH245_266_02.raw Raw
20190627_BBH245_266_03.raw Raw
20190627_BBH245_288_01.raw Raw
20190627_BBH245_288_02.raw Raw
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Publications

Acyldepsipeptide Probes Facilitate Specific Detection of Caseinolytic Protease P Independent of Its Oligomeric and Activity State.

Eyermann Barbara B   Meixner Maximilian M   Brötz-Oesterhelt Heike H   Antes Iris I   Sieber Stephan A SA  

Chembiochem : a European journal of chemical biology 20200107 1-2


Caseinolytic protease P (ClpP) is a tetradecameric peptidase that assembles with chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) are small-molecule mimics of ClpX that bind into hydrophobic pockets on the apical site of the complex, thereby activating ClpP. Detection of ClpP has so far been facilitated with active-site-directed probes which depend on the activity and oligomeric state of the complex. To expand the scope of ClpP labeling, we took a stepwise syntheti  ...[more]

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