LapD is a Bis-(3′,5′)-Cyclic Dimeric GMP-Binding Protein that Regulates Surface Attachment by Pseudomonas Fluorescens Pf0–1
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.