Structure of the VipA/B type VI secretion complex suggests a contraction-state-specific recycling mechanism

Sebastian Kube, Nicole Kapitein, Tomasz Zimniak, Franz Herzog, Axel Mogk, Petra Wendler

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

Abstract

The bacterial type VI secretion system is a multicomponent molecular machine directed against eukaryotic host cells and competing bacteria. An intracellular contractile tubular structure that bears functional homology with bacteriophage tails is pivotal for ejection of pathogenic effectors. Here, we present the 6Å cryoelectron microscopy structure of the contracted Vibrio cholerae tubule consisting of the proteins VipA and VipB. We localized VipA and VipB in the protomer and identified structural homology between the C-terminal segment of VipB and the tail-sheath protein of T4 phages. We propose that homologous segments in VipB and T4 phages mediate tubule contraction. We show that in type VI secretion, contraction leads to exposure of the ClpV recognition motif, which is embedded in the type VI-specific four-helix-bundle N-domain of VipB. Disaggregation of the tubules by the AAA+ protein ClpV and recycling of the VipA/B subunits are thereby limited to the contracted state.

OriginalspracheEnglisch
Seiten (von - bis)20-30
Seitenumfang11
FachzeitschriftCell Reports
Jahrgang8
Ausgabenummer1
DOIs
PublikationsstatusVeröffentlicht - 10 Juli 2014
Extern publiziertJa

Fingerprint

Untersuchen Sie die Forschungsthemen von „Structure of the VipA/B type VI secretion complex suggests a contraction-state-specific recycling mechanism“. Zusammen bilden sie einen einzigartigen Fingerprint.

Dieses zitieren