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. 2021 Mar 11;10(3):623. doi: 10.3390/cells10030623

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Identification of mono-ADP-ribosylated peptides in bacterial expressed and purified ERα. (A) Representative SDS-PAGE of GST-PARP7 and ERα prior to LC/MS analysis. (B) A schematic representation of the domain structure of ERα. Location of ADP-ribosylated peptides are denoted by yellow rectangles. Peptide sequences are numbered from the unmodified full-length protein. (C) The MS2 spectrum of the trypsin generated ion at m/z 940.855. (D) The MS2 spectrum of the trypsin generated ion at m/z 920.705. (E) The MS2 spectrum of the trypsin generated ion at m/z 796.657. (F) Relative levels of modification (in percentage) of ADP-ribosylated peptides identified by M/S in ERα.