1. SptP106–136 plays a role in the complex formation with SptP-specific chaperone SicP
- Author
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Shinobu Takeuchi, Kenji Oosawa, Fumio Hayashi, Eri Inobe, Kensuke Okimori, and Yurie Kawashima
- Subjects
Salmonella typhimurium ,Complex formation ,Virulence ,Applied Microbiology and Biotechnology ,Biochemistry ,Analytical Chemistry ,Type three secretion system ,Bacterial Proteins ,Humans ,Secretion ,Molecular Biology ,biology ,Effector ,Organic Chemistry ,General Medicine ,In vitro ,Protein Structure, Tertiary ,Cell biology ,Chaperone (protein) ,Host-Pathogen Interactions ,Salmonella Infections ,biology.protein ,Protein Tyrosine Phosphatases ,Molecular Chaperones ,Protein Binding ,Biotechnology - 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.
- Published
- 2014
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