Beta-ketoadipate enol-lactone hydrolases I and II from Acinetobacter calcoaceticus

Patel, Ramesh N.; Mazumdar, Suchismita; Ornston, L N

doi:10.1016/s0021-9258(19)41104-6

Cited by 37 publications

(1 citation statement)

References 58 publications

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“…To investigate how the distance between neighboring cells affects contact‐dependent assembly, we determined sheath formation dynamics in the A. baylyi BD4 strain, which produces more capsule than A. baylyi ADP1 (Heidelberger et al , 1969 ; Juni & Janik, 1969 ; Juni, 1972 ; Patel et al , 1975 ). Indeed, there were gaps (~220 nm) between cells of A. baylyi BD4 while no such large gaps were detectable in A. baylyi ADP1 or BD4 mutants lacking galU, a factor required for capsule production (Fig EV2A ).…”

Section: Resultsmentioning

confidence: 99%

Subcellular localization of Type VI secretion system assembly in response to cell–cell contact

et al. 2022

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Bacteria require a number of systems, including the type VI secretion system (T6SS), for interbacterial competition and pathogenesis. The T6SS is a large nanomachine that can deliver toxins directly across membranes of proximal target cells. Since major reassembly of T6SS is necessary after each secretion event, accurate timing and localization of T6SS assembly can lower the cost of protein translocation. Although critically important, mechanisms underlying spatiotemporal regulation of T6SS assembly remain poorly understood. Here, we used super-resolution live-cell imaging to show that while Acinetobacter and Burkholderia thailandensis can assemble T6SS at any site, a significant subset of T6SS assemblies localizes precisely to the site of contact between neighboring bacteria. We identified a class of diverse, previously uncharacterized, periplasmic proteins required for this dynamic localization of T6SS to cell-cell contact (TslA). This precise localization is also dependent on the outer membrane porin OmpA. Our analysis links transmembrane communication to accurate timing and localization of T6SS assembly as well as uncovers a pathway allowing bacterial cells to respond to cell-cell contact during interbacterial competition.

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