Rebuilding Ring-Type Assembly of Peroxiredoxin by Chemical Modification
Direct control of the protein quaternary structure (QS) is challenging owing to the complexity of the 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 reconst...
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| Veröffentlicht in: | Bioconjugate chemistry 2021-01, Vol.32 (1), p.153-160 |
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| container_title | Bioconjugate chemistry |
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| creator | Himiyama, Tomoki Tsuchiya, Yuko Yonezawa, Yasushige Nakamura, Tsutomu |
| description | Direct control of the protein quaternary structure (QS) is challenging owing to the complexity of the 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 the protein assembly state. |
| doi_str_mv | 10.1021/acs.bioconjchem.0c00587 |
| format | Article |
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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. 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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. 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| language | eng |
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| source | ACS Publications |
| subjects | Amino acids Assembly Chemical modification Dimers Mutants Mutation Peroxiredoxin Protein interaction Protein structure Proteins Quaternary structure Rebuilding Serine Structural analysis |
| title | Rebuilding Ring-Type Assembly of Peroxiredoxin by Chemical Modification |
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