the bona fide substrate membrane docking/translocation module-embedded monoubiquitinated PEX5 interacts directly with both enzyme forms PEX1 and PEX6 through its ubiquitin moiety. The PEX5 polypeptide chain is globally unfolded during the ATP-dependent extraction event
the enzyme degrades soluble unfolded and non-assembled peroxisomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
the enzyme degrades soluble unfolded and non-assembled peroxisomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
the enzyme degrades soluble unfolded and non-assembled peroxisomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein
Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease
Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease
Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished
a set of proteins, PEX1, PEX6 and a poorly conserved tail-anchored membrane protein, is required to extract monoubiquitinated PEX5 from the docking/translocation module. The PEX15 fragment is acting as a substrate for PEX1/PEX6
the Pex1p/Pex6p enzyme complex is able to bind efficiently to Pex15p in vivo. Pex6p mediates binding to the cytosolic part of Pex15p via a direct interaction
the protein translocase unfolds Pex15 in a pore-loop-dependent and ATP-hydrolysis-dependent manner. Pex15 binds the N-terminal domains of enzyme Pex6, before its C-terminal disordered region engages with the pore loops of the motor, which then processively threads Pex15 through the central pore. Furthermore, Pex15 directly binds the cargo receptor Pex5, linking Pex1/Pex6 to other components of the peroxisomal import machinery