PXD027954

PXD027954 is an original dataset announced via ProteomeXchange.

Title	Substrate profiling of mitochondrial caseinolytic protease P via a site-specific photocrosslinking approach
Description	The function of proteases is mainly determined by the substrates they are processing. However, substrate identification remains a challenging task. Here, we used genetic code expansion to incorporate a diazirine-lysine amino acid (DiazK) at selected positions of mitochondrial caseinolytic protease P (ClpP) in mammalian cells and determined its substrate scope by proteomic analyses after UV-light dependent photocrosslink. The results confirm its major involvement in maintaining the overall mitochondrial protein homeostasis as evident from alternative approaches. Additionally, novel putative substrates were identified revealing the highly complementary nature of this approach. Furthermore, this allows for the identification of changing substrate dynamics in an unbiased manner. Induction of oxidative stress with rotenone followed by identification of unique proteins corroborate its role in mitochondrial stress response. We hypothesize, that the oxidative stress is counteracted by processing proteins, which are involved in respiratory chain complex proteins synthesis and maturation as well as catabolic enzymes respectively.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:04:48.141.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Thomas Gronauer
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-08-16 06:20:01	ID requested
1	2023-08-21 21:48:21	announced
⏵ 2	2023-11-14 09:04:54	announced	2023-11-14: Updated project metadata.

Nguyen TA, Gronauer TF, Nast-Kolb T, Sieber SA, Lang K, Substrate Profiling of Mitochondrial Caseinolytic Protease P via a Site-Specific Photocrosslinking Approach. Angew Chem Int Ed Engl, 61(10):e202111085(2022) [pubmed]

submitter keyword: mtUPR, Mitochondria, photoaffinity crosslinking,ClpXP, Orbitrap Fusion

Stephan Axel Sieber
contact affiliation	Technical University of Munich, Department of Chemistry, Chair of Organic Chemistry 2, Germany
contact email	stephan.sieber@tum.de
lab head
Thomas Gronauer
contact affiliation	TU Munich Department of Chemistry Chair of Organic Chemistry 2 Lichtenbergstraße 4 85748 Garching Germany
contact email	thomas.gronauer@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/2023/08/PXD027954

PRIDE project URI

• PRIDE
  1. PXD027954
     1. Label: PRIDE project
     2. Name: Substrate profiling of mitochondrial caseinolytic protease P via a site-specific photocrosslinking approach