Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Katja Bernfur  

LAB HEAD: Herwig Schüler

PROVIDER: PXD067296 | Pride | 2025-09-29

REPOSITORIES: Pride