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Verfasst von:Kapitein, Nicole [VerfasserIn]   i
 Bönemann, Gabriele [VerfasserIn]   i
 Pietrosiuk, Aleksandra [VerfasserIn]   i
 Seyffer, Fabian [VerfasserIn]   i
 Haußer-Siller, Ingrid [VerfasserIn]   i
 Krijnse-Locker, Jacomine [VerfasserIn]   i
 Mogk, Axel [VerfasserIn]   i
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
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