title: PPIase independent chaperone-like function of recombinant human Cyclophilin A during arginine kinase refolding.
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.
authors: College of Life Sciences, Hubei Normal University, Huangshi, Hubei 435002, PR China.
authors: Xin-Chao
authors: XC
authors: Zhang
authors: Wei-Dong
authors: WD
authors: Wang
authors: Jin-Song
authors: JS
authors: Wang
authors: Ji-Cheng
authors: JC
authors: Pan
mesh_terms: D001122:Arginine Kinase / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D021984:Cyclophilin A / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D009842:Oligopeptides / Q000737:chemistry; D011485:Protein Binding; D015202:Protein Engineering; D058849:Protein Refolding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013499:Surface Properties
chemical_list: D018832:Molecular Chaperones; D009842:Oligopeptides; D011994:Recombinant Proteins; C043307:succinyl-alanyl-alanyl-prolyl-phenylalanine-4-nitroanilide; D001122:Arginine Kinase; D021984:Cyclophilin A