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Rebuilding Ring-Type Assembly of Peroxiredoxin by Chemical Modification

preprint
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.

Funding

Development of novel artificial metal enzymes based on hyperthermophilic archaeon derived peroxiredoxin

Japan Society for the Promotion of Science

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Function switching by controlling the quaternary structure of cyclic proteins

Japan Society for the Promotion of Science

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A novel supramolecular complex of peroxiredoxin

Japan Society for the Promotion of Science

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BINDS from AMED JP20am0101110 (support number 2578)

History

Email Address of Submitting Author

t-himiyama@aist.go.jp

Institution

National Institute for Advanced Industrial Science and Technology

Country

Japan

ORCID For Submitting Author

0000-0001-5252-1834

Declaration of Conflict of Interest

There are no conflicts to declare.

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