Abstract
The type VI secretion system (T6SS) inhibits the growth of neighboring bacterial cells through a contact-mediated mechanism. Here, we describe a detailed characterization of the protein localization dynamics in the Pseudomonas aeruginosa T6SS. It has been proposed that the type VI secretion process is driven by a conformational-change-induced contraction of the T6SS sheath. However, although the contraction of an optically resolvable TssBC sheath and the subsequent localization of ClpV are observed in Vibrio cholerae, coordinated assembly and disassembly of TssB and ClpV are observed without TssB contraction in P. aeruginosa. These dynamics are inconsistent with the proposed contraction sheath model. Motivated by the phenomenon of dynamic instability, we propose a new model in which ATP hydrolysis, rather than conformational change, generates the force for secretion.
Original language | English |
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Article number | e00744-17 |
Journal | Journal of bacteriology |
Volume | 200 |
Issue number | 11 |
DOIs | |
State | Published - Jun 1 2018 |
Keywords
- Bacterial cell biology
- Quantitative fluorescent imaging
- Subcellular dynamics
- T6SS