Document Detail


Organization and coordinated assembly of the type III secretion export apparatus.
MedLine Citation:
PMID:  20876096     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Type III protein secretion systems are unique bacterial nanomachines with the capacity to deliver bacterial effector proteins into eukaryotic cells. These systems are critical to the biology of many pathogenic or symbiotic bacteria for insects, plants, animals, and humans. Essential components of these systems are multiprotein envelope-associated organelles known as the needle complex and a group of membrane proteins that compose the so-called export apparatus. Here, we show that components of the export apparatus associate intimately with the needle complex, forming a structure that can be visualized by cryo-electron microscopy. We also show that formation of the needle complex base is initiated at the export apparatus and that, in the absence of export apparatus components, there is a significant reduction in the levels of needle complex base assembly. Our results show a substantial coordination in the assembly of the two central elements of type III secretion machines.
Authors:
Samuel Wagner; Lisa Königsmaier; María Lara-Tejero; Matthew Lefebre; Thomas C Marlovits; Jorge E Galán
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2010-09-27
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  107     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-10-13     Completed Date:  2010-11-22     Revised Date:  2014-04-25    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  17745-50     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / metabolism*
Blotting, Western
Cryoelectron Microscopy
Image Processing, Computer-Assisted
Immunoprecipitation
Membrane Transport Proteins / metabolism*
Multiprotein Complexes / metabolism*,  ultrastructure
Salmonella typhimurium / metabolism,  physiology*,  ultrastructure
Secretory Pathway / physiology*
Grant Support
ID/Acronym/Agency:
AI30492/AI/NIAID NIH HHS; R01 AI030492/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Membrane Transport Proteins; 0/Multiprotein Complexes; 0/PrgH protein, Salmonella typhimurium; 0/invG protein, Salmonella typhimurium
Comments/Corrections

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