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Rebuilding Ring-Type Assembly of Peroxiredoxin by Chemical Modification

submitted on 29.09.2020 and posted on 30.09.2020 by Tomoki Himiyama, Yuko Tsuchiya, Yasushige Yonezawa, Tsutomu Nakamura
Direct control of protein quaternary structure (QS) is challenging owing to the complexity of protein structure. As a protein with a characteristic QS, peroxiredoxin from Aeropyrum pernix K1 (ApPrx) forms a decamer, wherein five dimers associate to form a ring. Here, we disrupted and reconstituted ApPrx QS via amino acid mutations and chemical modifications targeting hot spots for protein assembly. The decameric QS of an ApPrx* mutant, wherein all cysteine residues in wild-type ApPrx were mutated to serine, was destructed to dimers via an F80C mutation. The dimeric ApPrx*F80C mutant was then modified with a small molecule and successfully assembled as a decamer. Structural analysis confirmed that an artificially installed chemical moiety potentially facilitates suitable protein-protein interactions to rebuild a native structure. Rebuilding of dodecamer was also achieved through an additional amino acid mutation. This study describes a facile method to regulate protein assembly state.


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BINDS from AMED JP20am0101110 (support number 2578)


Email Address of Submitting Author


National Institute for Advanced Industrial Science and Technology



ORCID For Submitting Author


Declaration of Conflict of Interest

There are no conflicts to declare.


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