Record Details
Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP
ScholarsArchive at Oregon State University
| Field | Value |
|---|---|
| Title | Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP |
| Names |
Chatterjee, Debashree
(creator) Cooley, Richard B. (creator) Boyd, Chelsea D. (creator) Mehl, Ryan A. (creator) O'Toole, George A. (creator) Sondermann, Holger (creator) |
| Date Issued | 2014-09-02 (iso8601) |
| Note | 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/. |
| Abstract | 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. |
| Genre | Article |
| Access Condition | http://creativecommons.org/licenses/by/3.0/us/ |
| Identifier | 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 |
