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

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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 co...

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Main Authors: Kapitein, Nicole (Author) , Bönemann, Gabriele (Author) , Pietrosiuk, Aleksandra (Author) , Seyffer, Fabian (Author) , Haußer-Siller, Ingrid (Author) , Krijnse-Locker, Jacomine (Author) , Mogk, Axel (Author)
Format: Article (Journal)
Language:English
Published: 3 February 2013
In: Molecular microbiology
Year: 2013, Volume: 87, Issue: 5, Pages: 1013-1028
ISSN:1365-2958
DOI:https://doi.org/10.1111/mmi.12147
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/https://doi.org/10.1111/mmi.12147
Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/mmi.12147
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Author Notes:Nicole Kapitein, Gabriele Bönemann, Aleksandra Pietrosiuk, Fabian Seyffer, Ingrid Hausser, Jacomine Krijnse Locker and Axel Mogk
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Summary: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.
Item Description:Gesehen am 21.04.2021
Physical Description:Online Resource
ISSN:1365-2958
DOI:https://doi.org/10.1111/mmi.12147

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