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Updated: Apr 24, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
Published on: June 26, 2020
SptP106-136 plays a role in the complex formation with SptP-specific chaperone SicP
Fumio Hayashi1, Yurie Kawashima, Shinobu Takeuchi
1a Division of Molecular Science, Faculty of Science and Technology , Gunma University , Kiryu , Japan.
Abstract:
SptP is a virulence effector protein of Salmonella that is involved in bacterial invasion into a host cell. For effective secretion, SptP forms a complex with SptP-specific chaperone SicP through its chaperone-binding domain, residues 35-139. Here, we suggest the possibility that residues 106-136 of SptP are important for complex formation with SicP by in vitro reconstitution experiments.
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