2014
Type VI secretion and bacteriophage tail tubes share a common assembly pathway
Abstract: The Type VI secretion system (T6SS) is a widespread macromolecular structure that delivers protein effectors to both eukaryotic and prokaryotic recipient cells. The current model describes the T6SS as an inverted phage tail composed of a sheath-like structure wrapped around a tube assembled by stacked Hcp hexamers. Although recent progress has been made to understand T6SS sheath assembly and dynamics, there is no evidence that Hcp forms tubes in vivo. Here we show that Hcp interacts with TssB, a component of t…
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Cited by 123 publications
(145 citation statements)
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“…1g ). A similar hexameric ring stacking which forms a nanotube was previously reported 21 22 25 26 .…”
Section: Resultssupporting
confidence: 78%
“…1g ). A similar hexameric ring stacking which forms a nanotube was previously reported 21 22 25 26 .…”
Section: Resultssupporting
confidence: 78%
“…1a). This pattern had been reported for T6SSs in V. cholerae 8 and EAEC 27 and represents the canonical model of firing of T6SSs (and CISs in general). Strikingly, 17% of the monitored events showed T6SS sheaths that entirely contracted toward the distal end (Fig.…”
Section: Resultssupporting
confidence: 77%
“…Three classes of contraction events were observed. Canonical contraction (observed previously 8,27 ) occurred toward the proximal end ( a ). Non-canonical opposite contraction occurred toward the distal end ( b ), or the T6SS split and contraction occurred simultaneously toward the proximal and distal ends ( c ).…”
Section: Resultsmentioning
confidence: 67%
“…We thus propose that the hub formed by the VgrG gp27-like domain trimer serves as an adaptor to recruit the first Hcp hexameric ring and thus initiates the assembly of the inner tube. In agreement with this proposal, in vivo tube formation assays have shown that the Hcp1 tube does not assemble properly in absence of vgrG1 [47].…”
Section: Discussionsupporting
confidence: 72%
