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Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP

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https://ir.library.oregonstate.edu/concern/articles/qj72p9179

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  • Stable surface adhesion of cells is one of the early pivotal steps in bacterial biofilm formation, a prevalent adaptation strategy in response to changing environments. In Pseudomonas fluorescens, this process is regulated by the Lap system and the second messenger cyclic-di-GMP. High cytoplasmic levels of cyclic-di-GMP activate the transmembrane receptor LapD that in turn recruits the periplasmic protease LapG, preventing it from cleaving a cell surface-bound adhesin, thereby promoting cell adhesion. In this study, we elucidate the molecular basis of LapG regulation by LapD and reveal a remarkably sensitive switching mechanism that is controlled by LapD's HAMP domain. LapD appears to act as a coincidence detector, whereby a weak interaction of LapG with LapD transmits a transient outside-in signal that is reinforced only when cyclic-di-GMP levels increase. Given the conservation of key elements of this receptor system in many bacterial species, the results are broadly relevant for cyclic-di-GMP- and HAMP domain-regulated transmembrane signaling.
  • This is the publisher’s final pdf. The published article is copyrighted by the author(s) and published by eLife Sciences Publications Ltd. The published article can be found at: http://elifesciences.org/.
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  • Chatterjee, D., Cooley, R. B., Boyd, C. D., Mehl, R. A., O'Toole, G. A., & Sondermann, H. (2014). Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP. eLife, 3, e03650. doi:10.7554/eLife.03650
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  • Part of this work is based upon research conducted at the Cornell High Energy Synchrotron Source (CHESS), which is supported by the National Science Foundation and the National Institutes of Health/National Institute of General Medical Sciences under NSF award DMR-1332208, using the Macromolecular Diffraction at CHESS (MacCHESS) facility, which is supported by award GM-103485 from the National Institute of General Medical Sciences, National Institutes of Health. Our work was supported by the NIH under grants R01-AI097307 (HS/GAO), F32-GM108440 (RBC), and T32-GM08704 (CDB), by the NSF under grant MCB9984521 (GAO), and by a PEW scholar award in Biomedical Sciences (HS).
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