PXD026605-1

PXD026605 is an original dataset announced via ProteomeXchange.

Title	Listeria monocytogenes utilizes the ClpP1/2 proteolytic machinery for fine-tuned substrate degradation under heat stress
Description	Listeria monocytogenes exhibits two ClpP isoforms (ClpP1/ClpP2) which assemble into a heterooligomeric complex with enhanced proteolytic activity. Herein, we demonstrate that the formation of this complex depends on temperature and reaches a maximum ratio of about 1:1 at heat shock conditions, while almost no complex formation occurred below 4°C. In order to decipher the role of the two isoforms at elevated temperatures, we constructed L. monocytogenes ClpP1, ClpP2 and ClpP1/2 knockout strains and analyzed their protein regulation in comparison to the wild type (WT) strain via whole proteome mass-spectrometry (MS) at 37 °C and 42 °C. While ΔclpP1 strain only altered the expression of very few proteins, ΔclpP2 and ΔclpP1/2 strains revealed the dysregulation of many proteins at both temperatures. These effects were corroborated by crosslinking co-immunoprecipitation MS analysis. Thus, while ClpP1 serves as a mere enhancer of protein degradation in the heterocomplex, ClpP2 is essential for ClpX binding and thus functions as a gatekeeper for substrate entry. Applying an integrated proteomic approach combining whole proteome and co immunoprecipitation datasets, several putative ClpP2 substrates were identified in the context of different temperatures and discussed with regards to their function in cellular pathways such as the SOS response.
HostingRepository	PRIDE
AnnounceDate	2022-09-20
AnnouncementXML	Submission_2022-09-20_10:20:51.293.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Konstantin Eckel
SpeciesList	scientific name: Listeria monocytogenes EGD-e; NCBI TaxID: 169963;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-06-09 22:56:23	ID requested
⏵ 1	2022-09-20 10:20:51	announced
2	2023-11-14 08:52:26	announced	2023-11-14: Updated project metadata.

10.1039/D2CB00077F;

submitter keyword: Listeria monocytogenes, proteolysis, XL-co-IP, ClpP, whole proteome

Stephan Axel Sieber
contact affiliation	Department of Chemistry, Chair of Organic Chemistry II, Center for Functional Protein Assemblies (CPA), Technical University of Munich, Ernst-Otto-Fischer Straße 8, 85748 Garching, Germany
contact email	stephan.sieber@tum.de
lab head
Konstantin Eckel
contact affiliation	Chair of Organic Chemistry II Technical University of Munich
contact email	k.eckel@tum.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD026605

PRIDE project URI

• PRIDE
  1. PXD026605
     1. Label: PRIDE project
     2. Name: Listeria monocytogenes utilizes the ClpP1/2 proteolytic machinery for fine-tuned substrate degradation under heat stress