Fig. 1: PARP15 dimerizes via its ART domain.
From: Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15
SEC-RALS/LALS analysis revealed that the PARP15 ART domain eluted as a dimer (a) from the size exclusion column whereas the ART domains of PARP14 (b) and PARP10 (c) were monomeric. The peak of the PARP15 macrodomain-2 - ART domain construct (m2-ART; d) contained both monomeric and dimeric species. The PARP15 macrodomain-2 (e) was a monomer. Further details are given in Supplementary Table 1. f Expected molecular weights of the respective monomers. g PARP15 ART and m2-ART constructs showed dimers on an SDS-PAGE gel after crosslinking with BS3. PARP15 m2 and PARP14 ART did not form dimers. Representative SDS-PAGE of n = 2 independent experiments. Size distribution of single particles of PARP15 ART (h; salmon) and PARP15 m2-ART (i; grey) in the nanomolar concentration range, observed by mass photometry. j Van Holde-Weischet integral distribution plot of sedimentation velocity experiments by analytical ultracentrifugation, conducted at four concentrations of ART domain and 40,000 rpm for 12 h. k Van Holde-Weischet integral distribution plot of a sedimentation velocity experiment conducted at 0.5 µM ART domain and 58,000 rpm for 5 h. Analysis of these data suggested a Kd for dimer formation of 313 nM. Source data are provided as a Source Data file.
