PXD016686 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Engineering Af1521 macro domain increases ADP-ribose binding affinity and leads to the identification of more ADP-ribosylated proteins |
Description | Protein ADP-ribosylation is a covalent, reversible post-translational modification that has important functions in several cellular mechanisms. The identification of modified proteins in cells has proven challenging and, due to the low abundance of protein ADP-ribosylation, has mainly been possible via enrichment methodologies using ADP-ribose binding domains. Here, using random mutagenesis and in vitro selection with an ADP-ribosylated histone peptide, we engineered the archaeal Af1521 macro domain to generate an engineered isoform containing nine mutations that displays significantly increased affinity towards ADP-ribose. Comparison of the wild-type and the engineered Af1521 macro domains using our proteomic ADP-ribosylome enrichment workflow demonstrated an increased identification rate of ADP-ribosylated proteins with the engineered Af1521. |
HostingRepository | PRIDE |
AnnounceDate | 2020-10-20 |
AnnouncementXML | Submission_2020-10-20_07:14:04.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Kathrin Nowak |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-12-11 00:21:34 | ID requested | |
⏵ 1 | 2020-10-20 07:14:05 | announced | |
Publication List
Nowak K, Rosenthal F, Karlberg T, B, ü, tepage M, Thorsell AG, Dreier B, Grossmann J, Sobek J, Imhof R, L, ü, scher B, Sch, ü, ler H, Pl, ü, ckthun A, Leslie Pedrioli DM, Hottiger MO, Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins. Nat Commun, 11(1):5199(2020) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: ADP-ribosylation, AP-MS, LC-MS/MS, Af1521 macro domain |
Contact List
Michael O. Hottiger |
contact affiliation | Department of Molecular Mechanisms of Disease, University of Zurich, Switzerland |
contact email | michael.hottiger@dmmd.uzh.ch |
lab head | |
Kathrin Nowak |
contact affiliation | University of Zurich |
contact email | kathrin.nowak@dmmd.uzh.ch |
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/2020/10/PXD016686 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD016686
- Label: PRIDE project
- Name: Engineering Af1521 macro domain increases ADP-ribose binding affinity and leads to the identification of more ADP-ribosylated proteins