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Fusion then fission: splitting and reassembly of an artificial fusion-protein nanocage.
Ohara, Naoya; Kawakami, Norifumi; Arai, Ryoichi; Adachi, Naruhiko; Ikeda, Akihito; Senda, Toshiya; Miyamoto, Kenji.
Affiliation
  • Ohara N; Department of Bioscience and Informatics, Faculty of Science and Technology, Keio University, Yokohama, Kanagawa 223-8522, Japan. norikawakami@bio.keio.ac.jp.
  • Kawakami N; Department of Bioscience and Informatics, Faculty of Science and Technology, Keio University, Yokohama, Kanagawa 223-8522, Japan. norikawakami@bio.keio.ac.jp.
  • Arai R; Department of Biomolecular Innovation, Institute for Biomedical Sciences, Interdisciplinary Cluster for Cutting Edge Research, Shinshu University, Ueda, Nagano 386-8567, Japan.
  • Adachi N; Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda, Nagano 386-8567, Japan.
  • Ikeda A; Structural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Oho, Tsukuba 305-0801, Japan.
  • Senda T; Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan.
  • Miyamoto K; Structural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Oho, Tsukuba 305-0801, Japan.
Chem Commun (Camb) ; 60(34): 4605-4608, 2024 Apr 23.
Article in En | MEDLINE | ID: mdl-38586927
ABSTRACT
A split-protein system is a simple approach to introduce new termini which are useful as modification sites in protein engineering, but has been adapted mainly for monomeric proteins. Here we demonstrate the design of split subunits of the 60-mer artificial fusion-protein nanocage TIP60. The subunit fragments successfully reformed the cage structure in the same manner as prior to splitting. One of the newly introduced terminals at the interior surface can be modified using a tag peptide and green fluorescent protein. Therefore, the termini could serve as a versatile modification site for incorporating a wide variety of functional peptides and proteins.

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Chem Commun (Camb) Journal subject: QUIMICA Year: 2024 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Chem Commun (Camb) Journal subject: QUIMICA Year: 2024 Document type: Article Affiliation country: Country of publication: