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PPIase independent chaperone‐like function of recombinant human Cyclophilin A during arginine kinase refolding
Author(s) -
Zhang Xin-Chao,
Wang Wei-Dong,
Wang Jin-Song,
Pan Ji-Cheng
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.01.028
Subject(s) - foldase , chaperone (clinical) , cyclophilin a , isomerase , cyclophilin , protein folding , biochemistry , chemistry , recombinant dna , arginine , arginine kinase , protein disulfide isomerase , peptidylprolyl isomerase , cypa , chemical chaperone , microbiology and biotechnology , biology , escherichia coli , amino acid , enzyme , endoplasmic reticulum , unfolded protein response , medicine , pathology , groel , gene
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.