An Oxygen-Sensing Diguanylate Cyclase and Phosphodiesterase Couple for c-di-GMP Control

Tuckerman, Jason R.; González, Gonzalo; Sousa, Eduardo Henrique Silva; Wan, Xuehua; Saito, Jennifer A.; Alam, Maqsudul; Gilles-Gonzalez, Marie Alda

doi:10.1021/bi901409g

Cited by 208 publications

(281 citation statements)

References 64 publications

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“…In P. aeruginosa, the diguanylate cyclases SiaD and WspR are activated upon exposure to SDS or contact with solid surfaces, respectively (15)(16)(17). In Escherichia coli, the activity of the DosCP cyclase/phosphodiesterase pair is modulated by oxygen availability (18), whereas diffusible signal factor was shown to activate c-di-GMP phosphodiesterase activity through the two-component regulatory system RpfG/C in Xanthomonas campestris (19). In addition, blue light was demonstrated to activate the c-di-GMP phosphodiesterase activity of BlrP1 in Klebsiella pneumoniae (20).…”

mentioning

confidence: 99%

Self-produced exopolysaccharide is a signal that stimulates biofilm formation inPseudomonas aeruginosa

Irie

Borlee

O'Connor

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

268

255

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Bacteria have a tendency to attach to surfaces and grow as structured communities called biofilms. Chronic biofilm infections are a problem because they tend to resist antibiotic treatment and are difficult to eradicate. Bacterial biofilms have an extracellular matrix that is usually composed of a mixture of polysaccharides, proteins, and nucleic acids. This matrix has long been assumed to play a passive structural and protective role for resident biofilm cells. Here we show that this view is an oversimplification and that the biofilm matrix can play an active role in stimulating its own synthesis. Working with the model biofilm bacterium Pseudomonas aeruginosa , we found that Psl, a major biofilm matrix polysaccharide for this species, acts as a signal to stimulate two diguanylate cyclases, SiaD and SadC, to produce the intracellular secondary messenger molecule c-di-GMP. Elevated intracellular concentrations of c-di-GMP then lead to the increased production of Psl and other components of the biofilm. This mechanism represents a unique positive feedback regulatory circuit, where the expression of an extracellular polysaccharide promotes biofilm growth in a manner analogous to autocrine signaling in eukaryotes.

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confidence: 99%

Self-produced exopolysaccharide is a signal that stimulates biofilm formation inPseudomonas aeruginosa

Irie

Borlee

O'Connor

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

268

255

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“…The structures of the globin fold of GCS enzymes are similar to those of myoglobin and hemoglobin but lack the entire D-and half of the E-helices of these proteins. Six heme-based oxygen sensor proteins, YddV (27,28), HemAT-Bs (29 -32), AvGReg (33), BpeGReg (34), GsGCS (35), and HemDGC (36), with the globin fold have been identified to date. Although both the sensor histidine kinase in the two-component system and GCS protein are important for bacteria to survive and/or to accommodate various stresses, no globin-coupled heme-regulated histidine kinases (GcHK) have been documented to date.…”

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confidence: 99%

Identification and Functional and Spectral Characterization of a Globin-coupled Histidine Kinase from Anaeromyxobacter sp. Fw109-5

Kitanishi

Kobayashi

Uchida

et al. 2011

Journal of Biological Chemistry

108

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Two-component signal transduction systems regulate numerous important physiological functions in bacteria. In this study we have identified, cloned, overexpressed, and characterized a dimeric full-length heme-bound (heme:protein, 1:1 stoichiometry) globin-coupled histidine kinase (AfGcHK) from Anaeromyxobacter sp. strain Fw109-5 for the first time. The Fe(III), Fe(II)-O2, and Fe(II)-CO complexes of the protein displayed autophosphorylation activity, whereas the Fe(II) complex had no significant activity. A H99A mutant lost heme binding ability, suggesting that this residue is the heme proximal ligand. Moreover, His-183 was proposed as the autophosphorylation site based on the finding that the H183A mutant protein was not phosphorylated. The phosphate group of autophosphorylated AfGcHK was transferred to Asp-52 and Asp-169 of a response regulator, as confirmed from site-directed mutagenesis experiments. Based on the amino acid sequences and crystal structures of other globin-coupled oxygen sensor enzymes, Tyr-45 was assumed to be the O2 binding site at the heme distal side. The O2 dissociation rate constant, 0.10 s−1, was substantially increased up to 8.0 s−1 upon Y45L mutation. The resonance Raman frequencies representing νFe-O2 (559 cm−1) and νO-O (1149 cm−1) of the Fe(II)-O2 complex of Y45F mutant AfGcHK were distinct from those of the wild-type protein (νFe-O2, 557 cm−1; νO-O, 1141 cm−1), supporting the proposal that Tyr-45 is located at the distal side and forms hydrogen bonds with the oxygen molecule bound to the Fe(II) complex. Thus, we have successfully identified and characterized a novel heme-based globin-coupled oxygen sensor histidine kinase, AfGcHK, in this study.

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“…In addition to GGDEF and EAL domains, Ea2862 also has a PAS domain that is predicted to sense small molecules such as metabolites and gases (33). Indeed, the automated PROKKA annotation program ascribed Ea2862 as a homolog of the oxygen-sensing protein DosP (34). In B. subtilis, loss of the EAL protein PdeH causes elevated levels of c-di-GMP that inhibit motility through the PilZ domain protein YpfA and the flagellar motor protein MotA (31,35,36).…”

Section: Significancementioning

confidence: 99%

Genomic sequencing-based mutational enrichment analysis identifies motility genes in a genetically intractable gut microbe

Bae

Mueller

Wong

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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A major roadblock to understanding how microbes in the gastrointestinal tract colonize and influence the physiology of their hosts is our inability to genetically manipulate new bacterial species and experimentally assess the function of their genes. We describe the application of population-based genomic sequencing after chemical mutagenesis to map bacterial genes responsible for motility in Exiguobacterium acetylicum, a representative intestinal Firmicutes bacterium that is intractable to molecular genetic manipulation. We derived strong associations between mutations in 57 E. acetylicum genes and impaired motility. Surprisingly, less than half of these genes were annotated as motility-related based on sequence homologies. We confirmed the genetic link between individual mutations and loss of motility for several of these genes by performing a large-scale analysis of spontaneous suppressor mutations. In the process, we reannotated genes belonging to a broad family of diguanylate cyclases and phosphodiesterases to highlight their specific role in motility and assigned functions to uncharacterized genes. Furthermore, we generated isogenic strains that allowed us to establish that Exiguobacterium motility is important for the colonization of its vertebrate host. These results indicate that genetic dissection of a complex trait, functional annotation of new genes, and the generation of mutant strains to define the role of genes in complex environments can be accomplished in bacteria without the development of species-specific molecular genetic tools. motility | mutagenesis | comparative genomics | gene annotation

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An Oxygen-Sensing Diguanylate Cyclase and Phosphodiesterase Couple for c-di-GMP Control

Cited by 208 publications

References 64 publications

Self-produced exopolysaccharide is a signal that stimulates biofilm formation inPseudomonas aeruginosa

Self-produced exopolysaccharide is a signal that stimulates biofilm formation inPseudomonas aeruginosa

Identification and Functional and Spectral Characterization of a Globin-coupled Histidine Kinase from Anaeromyxobacter sp. Fw109-5

Genomic sequencing-based mutational enrichment analysis identifies motility genes in a genetically intractable gut microbe

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