TL;DR
XcpS domains were identified that are important for species-specific functioning and thus represent putative interaction domains and the cytoplasmic loop of XcpS was found to be involved in the stabilization by XcpR and XcpY.
This study identified tyrosine phosphoprotein A (TypA) as a repressor that restricts expression of the T3SS in P. aeruginosa and reveals a novel molecular mechanism by which P. aeruginosa regulates T3SS.
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.
This review summarizes recent advances in the study of T6SSs that target eukaryotic cells, highlighting their roles in virulence, resistance to environmental predators, and microbial competition, and discusses T6SS-mediated interactions with protozoan predators, fungi, animal hosts and plants.
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.
Current knowledge on T9SS architecture and function is summarized, the embedded gliding machinery is described, and conceptual advances and open questions regarding the mechanisms, dynamics, and ecological implications of this unique system are highlighted.
The central role of sRNAs in the adaptive fitness of E. amylovora within host environments is underscored, with a particular focus on the Hfq-associated trans -encoded sRNAs ArcZ and RprA.
We use cookies to run the site and, with your consent, for analytics and to show ads. See our Cookie Policy.
