PXD015244

PXD015244 is an original dataset announced via ProteomeXchange.

Title	Acyldepsipeptide probes facilitate specific detection of caseinolytic protease P independent of its oligomeric and activity state
Description	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.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:05:21.692.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Barbara Hofbauer
SpeciesList	scientific name: Staphylococcus aureus; NCBI TaxID: 1280;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-08-30 03:55:30	ID requested
1	2020-05-26 14:31:17	announced
⏵ 2	2024-10-22 05:05:22	announced	2024-10-22: Updated project metadata.

10.1002/cbic.201900477;

Eyermann B, Meixner M, Br, ö, tz-Oesterhelt H, Antes I, Sieber SA, P Independent of Its Oligomeric and Activity State. Chembiochem, 21(1-2):235-240(2020) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: Thermo Fischer Q Exactive Orbitrap,photoaffinity labeling, S. aureus

Stephan A. Sieber
contact affiliation	Department of Chemistry Chair of Organic Chemistry II Technical University of Munich Germany
contact email	stephan.sieber@tum.de
lab head
Barbara Hofbauer
contact affiliation	Technische Universität München
contact email	b.hofbauer@tum.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD015244
     1. Label: PRIDE project
     2. Name: Acyldepsipeptide probes facilitate specific detection of caseinolytic protease P independent of its oligomeric and activity state