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