PXD067296-1

PXD067296 is an original dataset announced via ProteomeXchange.

Title	Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15
Description	The catalytic domain of PARP15 dimerizes, forming the same dimer interface in solution that had already been captured by X-ray crystallography of the domain. Furthermore, we show that the formation of dimers is a prerequisite for catalytic activity and that monomeric mutant variants of the domain were catalytically inactive. Our findings suggest a regulatory mechanism by which dimerization is linked to either target engagement or placement of a catalytic residue, rather than NAD+ co-substrate binding, and by which the two protomers of the dimer operate independent of one another.
HostingRepository	PRIDE
AnnounceDate	2025-09-29
AnnouncementXML	Submission_2025-09-29_04:27:21.069.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Katja Bernfur
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	Bruker Daltonics timsTOF series

Revision	Datetime	Status	ChangeLog Entry
0	2025-08-13 06:18:50	ID requested
⏵ 1	2025-09-29 04:27:21	announced

Dataset with its publication pending

submitter keyword: crosslinking mass spectrometry,PARP15

Herwig Schüler
contact affiliation	universitetslektor
contact email	herwig.schuler@biochemistry.lu.se
lab head
Katja Bernfur
contact affiliation	Lund University
contact email	katja.bernfur@biochemistry.lu.se
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD067296
     1. Label: PRIDE project
     2. Name: Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15