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. 2020 Nov 3;11:572419. doi: 10.3389/fmicb.2020.572419

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Copyright © 2020 Kaspy and Glaser.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Dimerization of YG4 and RelA. In vitro cross-linking reactions were performed by incubating the proteins and analyzing them by Western Blot. (+): with glutaraldehyde; (−): without glutaraldehyde. (A) Cross-linking of YG4 (left) and YG4-C638F (right). (B) From left to right: cross-linking of RelA, RelA and YG4, RelA, and YG4-C638F. (C,D) Mass spectrometry (MS)-MS analysis of digested YG4 peptides. (C) MS-MS analysis of YG4 dimers, digested without DTT reducing treatment, showing a fragment including an inter-chain S-S bond corresponding to Cys638-Cys638 (box); m/z = 1,147; (D) MS-MS analysis of reduced and digested YG4 dimers; note the absence of the fragment seen in (C; see box).