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A novel effector secretion mechanism based on proton-motive force-dependent type III secretion apparatus rotation.
MedLine Citation:
PMID:  23515444     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The type III secretion apparatus (T3SA) participates in the secretion of bacterial proteins called effectors, although the detailed mechanism of effector secretion remains unclear. T3SA and flagellum were shown to branch from a common ancestor and also show structural similarity. In addition, both T3SA-dependent effector secretion and flagellar rotation were reported to require proton-motive force (PMF) for activity. From these reports, we hypothesized that T3SA, like the flagellum, would rotate via PMF and that this rotation is responsible for effector secretion. To observe T3SA rotation, we constructed a novel observation system by modifying the tip of T3SA on bacterial cell membranes with an observation probe, which allowed documentation of T3SA rotation for the first time. T3SA rotation was stopped by the addition of a protonophore that decreases PMF. Moreover, increased viscosity of the observation medium inhibited both rotation of T3SA associated with beads and effector secretion. These results suggested that effector secretion would follow the PMF-dependent rotation of T3SA and could be inhibited by preventing T3SA rotation. Moreover, the motion-track analysis of bead rotation suggested that the T3SA needle might be flexible. Consequently, we propose a "rotational secretion model" as a novel effector secretion mechanism of T3SA.-Ohgita, T., Hayashi, N., Hama, S., Tsuchiya, H., Gotoh, N., Kogure, K. A novel effector secretion mechanism based on proton-motive force-dependent type III secretion apparatus rotation.
Authors:
Takashi Ohgita; Naoki Hayashi; Susumu Hama; Hiroyuki Tsuchiya; Naomasa Gotoh; Kentaro Kogure
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-3-20
Journal Detail:
Title:  FASEB journal : official publication of the Federation of American Societies for Experimental Biology     Volume:  -     ISSN:  1530-6860     ISO Abbreviation:  FASEB J.     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-3-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8804484     Medline TA:  FASEB J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
*Department of Biophysical Chemistry and †Department of Microbiology and Infection Control Science, Kyoto Pharmaceutical University, Kyoto, Japan.
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