English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Composition, formation, and regulation of the cytosolic c-ring, a dynamic component of the type III secretion injectisome

Diepold, A., Kudryashev, M., Delalez, N. J., Berry, R. M., & Armitage, J. P. (2015). Composition, formation, and regulation of the cytosolic c-ring, a dynamic component of the type III secretion injectisome. PLoS Biology, 13(1): e1002039. doi:10.1371/journal.pbio.1002039.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Diepold, Andreas1, Author
Kudryashev, Misha2, 3, Author              
Delalez, Nicolas J.1, Author
Berry, Richard M.4, Author
Armitage, Judith P.1, Author
Affiliations:
1Department of Biochemistry, University of Oxford, Oxford, United Kingdom, ou_persistent22              
2Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel, 4058 Basel, Switzerland, ou_persistent22              
3Focal Area Infection Biology, Biozentrum, University of Basel, 4056 Basel, Switzerland, ou_persistent22              
4Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, United Kingdom , ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: Many gram-negative pathogens employ a type III secretion injectisome to translocate effector proteins into eukaryotic host cells. While the structure of the distal "needle complex" is well documented, the composition and role of the functionally important cytosolic complex remain less well understood. Using functional fluorescent fusions, we found that the C-ring, an essential and conserved cytosolic component of the system, is composed of ~22 copies of SctQ (YscQ in Yersinia enterocolitica), which require the presence of YscQC, the product of an internal translation initiation site in yscQ, for their cooperative assembly. Photoactivated localization microscopy (PALM) reveals that in vivo, YscQ is present in both a free-moving cytosolic and a stable injectisome-bound state. Notably, fluorescence recovery after photobleaching (FRAP) shows that YscQ exchanges between the injectisome and the cytosol, with a t½ of 68 ± 8 seconds when injectisomes are secreting. In contrast, the secretin SctC (YscC) and the major export apparatus component SctV (YscV) display minimal exchange. Under non-secreting conditions, the exchange rate of YscQ is reduced to t½ = 134 ± 16 seconds, revealing a correlation between C-ring exchange and injectisome activity, which indicates a possible role for C-ring stability in regulation of type III secretion. The stabilization of the C-ring depends on the presence of the functional ATPase SctN (YscN). These data provide new insights into the formation and composition of the injectisome and present a novel aspect of type III secretion, the exchange of C-ring subunits, which is regulated with respect to secretion.

Details

show
hide
Language(s): eng - English
 Dates: 2014-08-282014-12-022015-01-15
 Publication Status: Published online
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1371/journal.pbio.1002039
PMID: 25591178
PMC: PMC4295842
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: PLoS Biology
  Other : PLoS Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: San Francisco, California, US : Public Library of Science
Pages: - Volume / Issue: 13 (1) Sequence Number: e1002039 Start / End Page: - Identifier: ISSN: 1544-9173
CoNE: https://pure.mpg.de/cone/journals/resource/111056649444170