Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion-Reference-Cited by-同舟云学术

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Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion

Published:2003-09-07 Issue:10 Volume:10 Page:789-793
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Evdokimov Artem G,Phan Jason,Tropea Joseph E,Routzahn Karen M,Peters Howard K,Pokross Matthew,Waugh David S

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsb982.pdf

Reference22 articles.

1. Aldridge, P. & Hughes, K.T. Regulation of flagellar assembly. Curr. Opin. Microbiol. 5, 160–165 (2002).

2. Fraser, G.M., Bennett, J.C.Q. & Hughes, C. Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly. Mol. Microbiol. 32, 569–580 (1999).

3. Auvray, F., Thomas, J., Fraser, G.M. & Hughes, C. Flagellin polymerisation control by a cytosolic export chaperone. J. Mol. Biol. 308, 221–229 (2001).

4. Bennett, J.C.Q. & Hughes, C. From flagellum assembly to virulence: the extended family of type III export chaperones. Trends. Microbiol. 8, 202–204 (2000).

5. Page, A.-L. & Parsot, C. Chaperones of the type III secretion pathway: jacks of all trades. Mol. Microbiol. 46, 1–11 (2002).

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1. Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone;Protein Science;2024-01-23

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