ClpV recycles VipA/VipB tubules and prevents non-productive tubule formation to ensure efficient type VI protein secretion

• Verfasst von: Kapitein, Nicole [VerfasserIn]
• Verfasst von: Bönemann, Gabriele [VerfasserIn]
• Verfasst von: Pietrosiuk, Aleksandra [VerfasserIn]
• Verfasst von: Seyffer, Fabian [VerfasserIn]
• Verfasst von: Haußer-Siller, Ingrid [VerfasserIn]
• Verfasst von: Krijnse-Locker, Jacomine [VerfasserIn]
• Verfasst von: 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
• Teil: year:2013
• Teil: number:5
• Teil: month:03
• Teil: pages:1013-1028
• Teil: 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
• DOI: doi:10.1111/mmi.12147
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1755592353

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.