PXD031245 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Proximity labelling and cryomill affinity purification compared for Trypanosoma brucei proteins with unconfined, semi-confined and confined localisation |
Description | Identification of protein-protein interactions is a major contributor for understanding protein function and elucidating molecular and cellular mechanisms. Two strategies are currently popular for identification of protein interaction partners directly from the cellular environment. Affinity purification (pulldown) isolates the protein of interest with the aid of a matrix that specifically captures the target and potential partners. In BioID, the protein of interest is fused to biotin ligase facilitating proximity biotinylation and biotinylated proteins are isolated under stringent conditions with streptavidin. Whilst clear that these two methods can provide insight, it is also apparent that they can reveal distinct interactomes, but the basis for these differences is less obvious. We compare these methods using four different trypanosome proteins as baits: the cytoplasmic poly(A) binding proteins PABP1 and PABP2, mRNA export receptor MEX67, that shuttles between the nucleus and the cytoplasm with predominant localisation at the nuclear pores, and the nucleoporin NUP158. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_07:42:33.446.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Martin Zoltner |
SpeciesList | scientific name: Trypanosoma brucei; NCBI TaxID: 5691; |
ModificationList | iodoacetamide derivatized residue |
Instrument | Q Exactive; Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-01-25 07:35:20 | ID requested | |
1 | 2022-11-30 07:02:39 | announced | |
⏵ 2 | 2023-11-14 07:42:37 | announced | 2023-11-14: Updated project metadata. |
Publication List
Moreira CMDN, Kelemen CD, Obado SO, Zahedifard F, Zhang N, Holetz FB, Gauglitz L, Dallagiovanna B, Field MC, Kramer S, Zoltner M, Impact of inherent biases built into proteomic techniques: Proximity labeling and affinity capture compared. J Biol Chem, 299(1):102726(2023) [pubmed] |
Keyword List
submitter keyword: cryomilling,Affinity purification, proteome, BioID, interactome |
Contact List
Martin Zoltner |
contact affiliation | Head of Drug Discovery and Evaluation Center for Research of Pathogenicity and Virulence of Parasites Charles University in Prague, BIOCEV Průmyslová 595 252 50 Vestec Czech Republic phone: +420 325 873 966 |
contact email | zoltnerm@natur.cuni.cz |
lab head | |
Martin Zoltner |
contact affiliation | Division of Biological Chemistry & Drug Discovery School of Life Sciences University of Dundee Dundee DD1 5EH |
contact email | m.zoltner@dundee.ac.uk |
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/2022/11/PXD031245 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD031245
- Label: PRIDE project
- Name: Proximity labelling and cryomill affinity purification compared for Trypanosoma brucei proteins with unconfined, semi-confined and confined localisation