Peter D. Newell

TL;DR: In this paper, the graphs for glycogen (left panel) and glucose (right panel) were inadvertently switched in the top row of Supplementary Fig. 5b in this article, the correct version of the figure appears below.

TL;DR: LapD is characterized, a unique c-di-GMP effector protein that controls biofilm formation by communicating intracellular c- DiGMP levels to the membrane-localized attachment machinery via its periplasmic domain and is shown to serve as the c- di-G MP receptor connecting environmental modulation of intrace cellular c-Di-Gmp levels by inorganic phosphate to regulation of LapA localization and thus surface commitment by P. fluorescens.

TL;DR: The microbial basis of host traits varies in both specificity and modularity; microbe-mediated reduction in glucose is relatively nonspecific and modular, while triglyceride content is influenced by interactions among microbes.

TL;DR: The results suggest that RapA lowers the level of c‐di‐GMP, which in turn inhibits the secretion of LapA, a large adhesion required for biofilm formation by P. fluorescens and suggest this strategy may be broadly applicable to other bacteria.

TL;DR: A novel paradigm in bacterial signal transduction is described: regulation of a periplasmic enzyme by an inner membrane signaling protein that binds a cytoplasmic second messenger in a c-di-GMP control circuit.