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Chapter 19 : Environmental Control of Cyclic Di-GMP Signaling in : from Signal to Output

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Abstract:

Recently it was shown that P concentration regulates biofilm formation by Pf0-1 through a cyclic di-GMP (c-di-GMP) signaling pathway. Study of this response has produced one of the more complete pictures of how c-di-GMP signaling can link an environmental signal to a complex biological output. This research supports the idea that c-di-GMP is a conserved modality in biofilm regulation, with distinct outputs in different organisms, and provides a paradigm for conditional, transcriptional control of c-di-GMP signaling pathways. The cellular c-di-GMP levels in wild-type (WT) and the rapA mutant were compared under P starvation conditions. While LapA was secreted by lapD mutants, it was not retained in the cell-associated protein fraction and was lost to the culture supernatant. This phenomenon is notably similar to what happens to LapA in these fractions when the WT is grown in low P, prompting investigation of LapD’s role in Pho regulon control of LapA localization, discussed. LapD and RapA both affect LapA localization to the cell surface, and was required for biofilm formation by the mutant. The description above represents the current extent of our knowledge about c-di-GMP signaling in strain Pf0-1. The Wsp chemosensory pathway regulates adherence and EPS production by strain SBW25 and PA01. Transcriptional regulation of RapA in Pf0-1 seems a relatively straightforward strategy for modulating c-di-GMP levels when compared to other mechanisms shown to regulate DGC and PDE activities, including allosteric activation, subcellular localization, and mRNA stability.

Citation: Newell P, O’Toole G. 2010. Environmental Control of Cyclic Di-GMP Signaling in : from Signal to Output, p 282-290. In Wolfe A, Visick K (ed), The Second Messenger Cyclic Di-GMP. ASM Press, Washington, DC. doi: 10.1128/9781555816667.ch19

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Figures

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Figure 1.

A schematic summarizing the current model for how phosphate concentration controls biofilm formation by is shown at the molecular (top) and microscopic (bottom) levels. Left: Low extracellar P is sensed by the PhoR/Pst system complex, and this leads to activation of the PhoR kinase and phosphorylation of PhoB. PhoB∼P forms a dimer and binds to the Pho Box sequence upstream of activating its transcription. The RapA protein cleaves c-di-GMP to form pGpG through its PDE activity, depleting cellular c-di-GMP pools. Decreased cellular c-di-GMP leads to dissociation of the nucleotide from the c-di-GMP effector LapD, and this signal promotes the egress of LapA to the culture supernatant. Cells cannot maintain stable surface attachments in low P. Right: Under high-P conditions RapA is not expressed, and c-di-GMP accumulates in the cell. LapD binds c-di-GMP and sends a signal promoting the maintenance of LapA on the cell surface. Cells can form irreversible attachments to the substratum and can go on to form a biofilm. IM, inner membrane; OM, outer membrane.

Citation: Newell P, O’Toole G. 2010. Environmental Control of Cyclic Di-GMP Signaling in : from Signal to Output, p 282-290. In Wolfe A, Visick K (ed), The Second Messenger Cyclic Di-GMP. ASM Press, Washington, DC. doi: 10.1128/9781555816667.ch19
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References

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Tables

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Table 1

Conservation of c-di-GMP signaling components and attachment factors among

Citation: Newell P, O’Toole G. 2010. Environmental Control of Cyclic Di-GMP Signaling in : from Signal to Output, p 282-290. In Wolfe A, Visick K (ed), The Second Messenger Cyclic Di-GMP. ASM Press, Washington, DC. doi: 10.1128/9781555816667.ch19

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