PXD016686-1

PXD016686 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2019-12-11 00:21:34	ID requested
⏵ 1	2020-10-20 07:14:05	announced

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]

curator keyword: Biological

submitter keyword: ADP-ribosylation, AP-MS, LC-MS/MS, Af1521 macro domain

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

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

• PRIDE
  1. PXD016686
     1. Label: PRIDE project
     2. Name: Engineering Af1521 macro domain increases ADP-ribose binding affinity and leads to the identification of more ADP-ribosylated proteins