Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded by Salmonella pathogenicity island 2
Author:
Funder
MEXT | Japan Society for the Promotion of Science
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference53 articles.
1. Assembly, structure, function and regulation of type III secretion systems;Deng;Nat. Rev. Microbiol,2017
2. Type III secretion: building and operating a remarkable nanomachine;Portaliou;Trends Biochem. Sci,2016
3. The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system;Lefebre;Proc. Natl. Acad. Sci. U.S.A,2014
4. Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica;Agrain;Mol. Microbiol,2005
5. The structure of a type 3 secretion system (T3SS) ruler protein suggests a molecular mechanism for needle length sensing;Bergeron;J. Biol. Chem,2016
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2. Secreted in a Type III Secretion System-Dependent Manner, EsaH and EscE Are the Cochaperones of the T3SS Needle Protein EsaG of Edwardsiella piscicida;mBio;2022-08-30
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4. Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N‐terminal YscX secretor domain;Molecular Microbiology;2022-02-08
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