PXD052663 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | An 8-Mercaptoquinoline Motif Enriches Minichromosome Maintenance Complex Components as Significant Metalloprotein Targets in Live Cells |
Description | Affinity-based probes are valuable tools for detecting binding interactions between small molecules and proteins in complex biological environments. Metalloproteins are a class of therapeutically significant biomolecules which bind metal ions as part of key structural or catalytic domains and are compelling targets for study. However, there is currently a limited range of chemical tools suitable for profiling the metalloproteome. Here, we describe the preparation and application of a novel, photoactivatable affinity based probe for detection of a subset of previously challenging to engage metalloproteins. The probe, bearing an 8 mercaptoquinoline metal chelator, was anticipated to engage several zinc metalloproteins, including the 26S proteasome subunit Rpn11. Upon translation of the labelling experiment to mammalian cell lysates, proteomic analysis revealed that several metalloproteins were competitively enriched. An 8-mercaptoquinoline diazirine probe was found to effectively enrich multiple components of the minichromosome maintenance complex, a zinc metalloprotein assembly with helicase activity essential to DNA replication. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_06:47:49.596.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Sean McKenna |
SpeciesList | scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-05-29 02:07:45 | ID requested | |
1 | 2024-06-27 22:11:02 | announced | |
⏵ 2 | 2024-10-22 06:47:50 | announced | 2024-10-22: Updated project metadata. |
Publication List
Keyword List
submitter keyword: photoaffinity labelling, affinity-based protein profiling, metalloenzymes,Affinity-based probes, metalloproteins |
Contact List
Professor Joanna F. McGouran |
contact affiliation | Schuler Assistant Professor In Translational Organic Chemistry, School of Chemistry, Trinity College Dublin, Republic of Ireland |
contact email | jmcgoura@tcd.ie |
lab head | |
Sean McKenna |
contact affiliation | Trinity College Dublin Leiden University |
contact email | mckenns8@tcd.ie |
dataset submitter | |
Full Dataset Link List
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/2024/06/PXD052663 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD052663
- Label: PRIDE project
- Name: An 8-Mercaptoquinoline Motif Enriches Minichromosome Maintenance Complex Components as Significant Metalloprotein Targets in Live Cells