Extended Data Fig. 3: Reconstitution of BRISC–SHMT2 complex.

a, Summary of limited proteolysis and Edman sequencing results indicating trypsin protease-labile regions for the BRCC45–MERIT40 complex (left) and the BRISC (right). Protease cleavage sites are shown as scissors. Unstructured Abraxas 2 regions are indicated as dashed lines. b, SDS–PAGE of BRISC and BRISCΔNΔC (representative of three independent experiments). c, DUB activity of BRISC (full length) and BRISCΔNΔC (truncated) against a fluorogenic K63-linked diUb substrate. Data are mean ± s.e.m. of three independent experiments carried out in duplicate. d, SHMT2ΔN(A285T) inhibition of BRISC and BRISCΔNΔC DUB activity. Data are mean ± s.e.m. of three independent experiments carried out in duplicate. Ninety-five per cent confidence intervals are shown in square brackets. e, Size-exclusion chromatography of the BRISCΔNΔC–SHMT2ΔN(A285T) complex (top) and Coomassie-stained SDS–PAGE of peak fractions (bottom). f, Native mass spectrometry of the BRISCΔNΔC–SHMT2ΔN(A285T) complex. Data in e, f are representative of three independent experiments.