| Online-Ressource |
Verfasst von: | Kapitein, Nicole [VerfasserIn]  |
| Bönemann, Gabriele [VerfasserIn]  |
| Pietrosiuk, Aleksandra [VerfasserIn]  |
| Seyffer, Fabian [VerfasserIn]  |
| Haußer-Siller, Ingrid [VerfasserIn]  |
| Krijnse-Locker, Jacomine [VerfasserIn]  |
| Mogk, Axel [VerfasserIn]  |
Titel: | ClpV recycles VipA/VipB tubules and prevents non-productive tubule formation to ensure efficient type VI protein secretion |
Verf.angabe: | Nicole Kapitein, Gabriele Bönemann, Aleksandra Pietrosiuk, Fabian Seyffer, Ingrid Hausser, Jacomine Krijnse Locker and Axel Mogk |
E-Jahr: | 2013 |
Jahr: | 3 February 2013 |
Umfang: | 16 S. |
Teil: | volume:87 |
| year:2013 |
| number:5 |
| month:03 |
| pages:1013-1028 |
| extent:16 |
Fussnoten: | Gesehen am 21.04.2021 |
Titel Quelle: | Enthalten in: Molecular microbiology |
Ort Quelle: | Oxford [u.a.] : Wiley-Blackwell, 1987 |
Jahr Quelle: | 2013 |
Band/Heft Quelle: | 87(2013), 5 vom: März, Seite 1013-1028 |
ISSN Quelle: | 1365-2958 |
Abstract: | The multicomponent type VI secretion system (T6SS) mediates the transport of effector proteins by puncturing target membranes. T6SSs are suggested to form a contractile nanomachine, functioning similar to the cell-puncturing device of tailed bacteriophages. The T6SS members VipA/VipB form tubular complexes and are predicted to function in analogy to viral tail sheath proteins by providing the energy for secretion via contraction. The ATPase ClpV disassembles VipA/VipB tubules in vitro, but the physiological relevance of tubule disintegration remained unclear. Here, we show that VipA/VipB tubules localize near-perpendicular to the inner membrane of Vibrio cholerae cells and exhibit repetitive cycles of elongation, contraction and disassembly. VipA/VipB tubules are decorated by ClpV in vivo and become static in ΔclpV cells, indicating that ClpV is required for tubule removal. VipA/VipB tubules mislocalize in ΔclpV cells and exhibit a reduced frequency of tubule elongation, indicating that ClpV also suppresses the spontaneous formation of contracted, non-productive VipA/VipB tubules. ClpV activity is restricted to the contracted state of VipA/VipB, allowing formation of functional elongated tubules at a T6SS assembly. Targeting of an unrelated ATPase to VipA/VipB is sufficient to replace ClpV function in vivo, suggesting that ClpV activity is autonomously regulated by VipA/VipB conformation. |
DOI: | doi:10.1111/mmi.12147 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/https://doi.org/10.1111/mmi.12147 |
| Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/mmi.12147 |
| DOI: https://doi.org/10.1111/mmi.12147 |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 1755592353 |
Verknüpfungen: | → Zeitschrift |
ClpV recycles VipA/VipB tubules and prevents non-productive tubule formation to ensure efficient type VI protein secretion / Kapitein, Nicole [VerfasserIn]; 3 February 2013 (Online-Ressource)