SptP106–136 plays a role in the complex formation with SptP-specific chaperone SicP-Reference-Cited by-同舟云学术

SptP106–136 plays a role in the complex formation with SptP-specific chaperone SicP

Published:2014-09-02 Issue:9 Volume:78 Page:1560-1563
ISSN:0916-8451
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Hayashi Fumio¹,Kawashima Yurie¹,Takeuchi Shinobu¹,Okimori Kensuke¹,Inobe Eri¹,Oosawa Kenji¹

Affiliation:

1. Division of Molecular Science, Faculty of Science and Technology, Gunma University, Kiryu, Japan

Abstract

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.

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/article-pdf/78/9/1560/36800810/bbb1560.pdf

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