7,672 research outputs found
Dialogical Skirmishes
Tan was guest editor for 'And Now China?', a special print edition of the Ctrl+P journal, which critically responded to the celebratory rhetoric’s of ‘China Now’ and other celebratory markers of China's global ascent in 2008. As well as the introductory article 'Dialogical Skirmishes', Tan also interviewed Hans Ulrich Obrist
Evidence for erbium-erbium energy migration in erbium(III) bis(perfluoro-p-tolyl)phosphinate
Copyright 2008 American Institute of Physics. This article may be downloaded for personal use only. Any other use requires prior permission of the author and the American Institute of Physics. This article appeared in Applied Physics Letters 92, 103303 (2008) and may be found at
Free thinking - running
We've been running for two million years give or take. Shahidha Bari and Laurence Scott explore contemporary running as solitary inspiration and communal activity with the Geographer and 1999 Scottish Hill Running Champion, Hayden Lorimer, the artists Kai Syng Tan and Angus Farquhar, and the literary scholar and bare-foot artiste, Vybarr Cregan-Reid. Conversation ranges from feeling empowered on city streets to teaming up with the wind to the horrid history of the treadmill and explore whether Running deserves better representation in the arts. Guests: Vybarr Cregan-Reid - author of Footnotes How Running Makes Us Human Angus Farquhar, Creative Director of NVA Public Art, author of a blog 'The Grim Runner' Hayden Lorimer Running Geographer Kai Syng Tan, Artist and curator of a biennial festival Run Run Run Producer: Jacqueline Smith
Contact-dependent growth inhibition (CDI) systems deploy a large family of polymorphic ionophoric toxins for inter-bacterial competition
Contact-dependent growth inhibition (CDI) is a widespread form of inter-bacterial competition mediated by CdiA effector proteins. CdiA is presented on the inhibitor cell surface and delivers its toxic C-terminal region (CdiA-CT) into neighboring bacteria upon contact. Inhibitor cells also produce CdiI immunity proteins, which neutralize CdiA-CT toxins to prevent auto-inhibition. Here, we describe a diverse group of CDI ionophore toxins that dissipate the transmembrane potential in target bacteria. These CdiA-CT toxins are composed of two distinct domains based on AlphaFold2 modeling. The C-terminal ionophore domains are all predicted to form five-helix bundles capable of spanning the cell membrane. The N-terminal "entry" domains are variable in structure and appear to hijack different integral membrane proteins to promote toxin assembly into the lipid bilayer. The CDI ionophores deployed by E. coli isolates partition into six major groups based on their entry domain structures. Comparative sequence analyses led to the identification of receptor proteins for ionophore toxins from groups 1 & 3 (AcrB), group 2 (SecY) and groups 4 (YciB). Using forward genetic approaches, we identify novel receptors for the group 5 and 6 ionophores. Group 5 exploits homologous putrescine import proteins encoded by puuP and plaP, and group 6 toxins recognize di/tripeptide transporters encoded by paralogous dtpA and dtpB genes. Finally, we find that the ionophore domains exhibit significant intra-group sequence variation, particularly at positions that are predicted to interact with CdiI. Accordingly, the corresponding immunity proteins are also highly polymorphic, typically sharing only ~30% sequence identity with members of the same group. Competition experiments confirm that the immunity proteins are specific for their cognate ionophores and provide no protection against other toxins from the same group. The specificity of this protein interaction network provides a mechanism for self/nonself discrimination between E. coli isolates
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