Fig. 1 | Nature Communications

Fig. 1

From: A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25

Fig. 1

Recombinant USP25 is produced as a tetramer or a dimer in E. coli. a Scheme of the USP25 protein domains. The construct for crystallization is from residues 18 to 714 (USP25NCD). b First preparative gel filtration purification of USP25 in Superdex 200 column, inset shows the SDS-PAGE of the indicated fractions. Anionic-exchange purification of the two peak fractions of the previous gel filtration, inset shows the SDS-PAGE of the dimer and tetramer fractions. Analytical gel filtration purification of the dimer and tetramer fractions of USP25 in Superdex 16 column. c Plot of the deubiquitinating activity assays of dimer and tetramer with Ub-AMC as a substrate. Non-denaturing native PAGE of the dimer and tetramer fractions of USP25NCD. All uncropped gels and blots are displayed in Supplementary Figure 12

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