Disease relevance of CPR3

• The high folding activities found previously originated from a contamination of the recombinant Cpr3 proteins with the Escherichia coli protein SlyD, a prolyl isomerase that co-purifies with His-tagged proteins [1].

High impact information on CPR3

• Here we show that Cpr3p, a cyclophilin in the matrix of yeast mitochondria, accelerates the refolding of a fusion protein that was synthesized in a reticulocyte lysate and imported into the matrix of isolated yeast mitochondria [2].
• This reduced rate of folding was also observed with mitochondria lacking Cpr3p [2].
• The rate of protein import was not affected by cyclosporin A or by deletion of Cpr3p [2].
• Deduced CPR2 and CPR3 amino acid sequences were 91% identical, but encoded isoforms divergent from CPR1 (72% identity) [3].
• A reinvestigation revealed that in fact these two mutations strongly decrease the prolyl isomerase activity of Cpr3 in both the peptide and the protein-folding assay [1].

Other interactions of CPR3

• We have isolated a yeast cyclophilin gene, CPR3, which encodes a presumptive mitochondrial isoform [4].

Analytical, diagnostic and therapeutic context of CPR3

• On the basis of the result of SDS-PAGE, PPI-II and PPI-III were highly purified and their molecular masses were estimated to be 16.5 and 17.2 kDa, respectively [5].

References