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Chaperoning activity of peroxiredoxins protects brain‐type creatine kinase under various stresses through specific interaction
Author(s) -
Rakhmetov Anar,
Lee Sang Pil,
Kim Kanghwa,
Chae Ho Zoon
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.lb136
Subject(s) - creatine kinase , chemistry , transition (genetics) , biochemistry , microbiology and biotechnology , chaperone (clinical) , biophysics , biology , gene , medicine , pathology
Peroxiredoxins (Prxs) are a family of peroxidase proteins which, although, exhibit chaperone activity due to the structural transition from dimer to decamer or high‐molecular weight complex. We have identified brain‐type creatine kinase (CKBB) as a Prx I binding protein from the heat‐stressed rat brain extracts. Co‐IP results from the transfected cells demonstrated that the interaction of CKBB with PrxII in addition to PrxI. PrxII showed much higher binding affinity to CKBB than PrxI under normal physiological condition as well as heat‐stressed condition. Prx II effectively protected the kinase activity of CKBB from oxidative inactivation and heat inactivation. This protection activity is not depends on the structural transition but depends on the site‐specific interaction. Thus, we suggest this chaperoning activity of Prx through the sitespecific interaction as “client specific chaperoning”, and that through structural transition as “general chaperoning”. For specific clients, Prx binds to their native state and provides the protection for maintain their native state. The beneficiary of chaperoning through structural transition (general chaperoning) opens to wide variety of clients, however, that through site‐specific interaction (client specific chaperoning) opens to very limited number of clients.