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. 2018 Aug 10;293(40):15458–15470. doi: 10.1074/jbc.RA118.003936

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© 2018 Schwerter et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 5. — In vitro deubiquitination of N-terminally ubiquitinated Ub_(1–6Δ)Pex5p. WT Ubp15p and the catalytically inactive mutant Ubp15p^C214A were treated with or without NEM and incubated with purified GST-tagged Ub_(1–6Δ)Pex5p. Samples taken at the indicated time points were subjected to SDS–PAGE and Coomassie staining (upper panels) or immunoblot analysis (lower panels) using antibodies against GST (red) and Pex5p (green). The increase of Pex5p and free GST-tagged ubiquitin (_GSTUb) in the sample containing the catalytically active and non-NEM-treated Ubp15p shows that the N-terminally ubiquitinated Ub_(1–6Δ)Pex5p is deubiquitinated by Ubp15p in vitro.