Proceedings of the National Academy of Sciences of the United States of America
Geisel School of Medicine
The second messenger cyclic dimeric GMP (c-di-GMP) regulates surface attachment and biofilm formation by many bacteria. For Pseudomonas fluorescens Pf0-1, c-di-GMP impacts the secretion and localization of the adhesin LapA, which is absolutely required for stable surface attachment and biofilm formation by this bacterium. In this study we characterize LapD, a unique c-di-GMP effector protein that controls biofilm formation by communicating intracellular c-di-GMP levels to the membrane-localized attachment machinery via its periplasmic domain. LapD contains degenerate and enzymatically inactive diguanylate cyclase and c-di-GMP phosphodiesterase (EAL) domains and binds to c-di-GMP through a degenerate EAL domain. We present evidence that LapD utilizes an inside-out signaling mechanism: binding c-di-GMP in the cytoplasm and communicating this signal to the periplasm via its periplasmic domain. Furthermore, we show that LapD serves as the c-di-GMP receptor connecting environmental modulation of intracellular c-di-GMP levels by inorganic phosphate to regulation of LapA localization and thus surface commitment by P. fluorescens.
Newell PD, Monds RD, O'Toole GA. LapD is a bis-(3',5')-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1. Proc Natl Acad Sci U S A. 2009 Mar 3;106(9):3461-6. doi: 10.1073/pnas.0808933106. Epub 2009 Feb 13. PMID: 19218451; PMCID: PMC2651287.
Dartmouth Digital Commons Citation
Newell, Peter D.; Monds, Russell D.; and O'Toole, George A., "LapD is a Bis-(3′,5′)-Cyclic Dimeric GMP-Binding Protein that Regulates Surface Attachment by Pseudomonas Fluorescens Pf0–1" (2009). Dartmouth Scholarship. 1506.