<<< Full experiment listing

PXD016686

PXD016686 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleEngineering Af1521 macro domain increases ADP-ribose binding affinity and leads to the identification of more ADP-ribosylated proteins
DescriptionProtein 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.
HostingRepositoryPRIDE
AnnounceDate2020-10-20
AnnouncementXMLSubmission_2020-10-20_07:14:04.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterKathrin Nowak
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListmonohydroxylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-12-11 00:21:34ID requested
12020-10-20 07:14:05announced
Publication List
Nowak K, Rosenthal F, Karlberg T, Bütepage M, Thorsell AG, Dreier B, Grossmann J, Sobek J, Imhof R, Lüscher B, Schüler H, Plückthun 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 affiliationDepartment of Molecular Mechanisms of Disease, University of Zurich, Switzerland
contact emailmichael.hottiger@dmmd.uzh.ch
lab head
Kathrin Nowak
contact affiliationUniversity of Zurich
contact emailkathrin.nowak@dmmd.uzh.ch
dataset submitter
Full Dataset Link List
Dataset FTP location
PRIDE project URI
Repository Record List
[ + ]