Extended Data Fig. 2: Pex2, Pex10, and Pex12 from S. cerevisiae or C. thermophilum form stoichiometric complexes. | Nature

Extended Data Fig. 2: Pex2, Pex10, and Pex12 from S. cerevisiae or C. thermophilum form stoichiometric complexes.

From: A peroxisomal ubiquitin ligase complex forms a retrotranslocation channel

Extended Data Fig. 2

Full-length S. cerevisiae Pex12 with an N-terminal streptavidin-binding peptide (SBP) tag was expressed together with full-length S. cerevisiae Pex10 and Pex2 in P. pastoris. The complex was purified with streptavidin beads and subjected to gel filtration. The upper panels show the absorbance profile. Fractions between the dashed lines were analyzed by SDS-PAGE and Coomassie blue staining (lower panels). The complex from C. thermophilum contained Pex2 (residues 107-455), lacking non-conserved residues at the N- and C-termini, and was purified in the same way. The results are representative of three biological repeats. For gel source data, see Supplementary Fig. 1.

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