1. PPIase independent chaperone-like function of recombinant human Cyclophilin A during arginine kinase refolding.
- Author
-
Zhang XC, Wang WD, Wang JS, and Pan JC
- Subjects
- Arginine Kinase metabolism, Binding Sites, Cyclophilin A genetics, Cyclophilin A metabolism, Escherichia coli genetics, Humans, Hydrophobic and Hydrophilic Interactions, Kinetics, Molecular Chaperones genetics, Molecular Chaperones metabolism, Mutagenesis, Site-Directed, Oligopeptides chemistry, Protein Binding, Protein Engineering, Protein Refolding, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Surface Properties, Arginine Kinase chemistry, Cyclophilin A chemistry, Molecular Chaperones chemistry
- Abstract
Whether Cyclophilin A (CyPA) functions as a foldase or a chaperone when assisting protein folding has long been argued. In this study, we engineered four variants of recombinant human Cyclophilin A (rhCyPA), all of which were inactive to tetrapeptide substrate Suc-AAPF-pNA. However, these variants were able to suppress aggregation during arginine kinase (AK) refolding as efficient as wild-type rhCyPA, especially, variant Q63A had even more efficiency to suppress aggregation and improve reactivation yields of AK. These results indicate that rhCyPA have peptidyl-prolyl cis-trans isomerase (PPIase) independent chaperone-like activity during AK folding. In addition, results suggest that surface hydrophobicity of rhCyPA can suppress AK aggregation and binding to rhCyPA hydrophobic active pocket is a prerequisite for chaperoning AK folding., (Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Published
- 2013
- Full Text
- View/download PDF