It is found that the leader peptide and the N-terminal 17 amino acid residues of mature XcpT could be functionally replaced by the corresponding part of PilA, which shows that this domain of the protein does not contain information for targeting to the Xcp system.
Key determinants of secretion specificity and endopilus stability are identified, revealing how minor sequence variations in conserved nanomachines drive functional adaptation to diverse environments.
Maylis Lejeune, S. Ivashchenko, Régine Dazzoni et al.· Structure· 0 citations
The extent to which chaperones are universally required for effector secretion is evaluated, through analysis of the conservation of chaperone sequence and structure, to discuss how these proteins interact with and support the secretion of diverse substrates.
Kyra Roepke, Alexia J Galsworthy, Adam Agbamu et al.· Microbiology· 0 citations
The T2SS is a fascinatingly complex “machine” whose contributing parts can vary and whose ability to recognize substrates is primarily conformational, involving spatially separated elements that interact with the T2SS apparatus through transient, multivalent interactions rather than a single dedicated binding motif.
N. Cianciotto, Joshua Mayoral, James A Garnett· Microbiology and Molecular B...· 0 citations
A "two-factor authentication" mechanism for pilus assembly in gram-positive bacteria is defined: class C sortases first verify pilin identity by forming a membrane-embedded interface that activates the enzyme, then they recognize the LPXTG motif to initiate loading and crosslinking.
Nicole A. Cheung, Reece M. Pawlaczyk, Brendan J. Mahoney et al.· Proceedings of the National...· 0 citations
It is shown that the last 12 residues of PilC, representing ∼1% of the protein, are both necessary and sufficient for pilus-tip localisation and filament biogenesis, defining the molecular basis of PilC/PilY1 function and localisation, and establishing a broadly applicable model for T4aP biogenesis.
Milica Denic, Morgane Wuckelt, V. Roig-Zamboni et al.· bioRxiv· 0 citations
TpeX is identified as a bactericidal, colicin-like pore-forming T6SS effector whose membrane activity is controlled by a cognate immunity protein, thereby expanding the repertoire of membrane-targeting weapons used by P. aeruginosa in interbacterial competition.
Chantal Soscia, Sébastien Reig, D. Lefebvre et al.· bioRxiv· 0 citations
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