Second Messenger-Mediated Adjustment of Bacterial Swimming Velocity

Boehm, Alex; Kaiser, Matthias J.; Li, Hui; Spangler, Christian; Kasper, Christoph; Ackermann, Martin; Kaever, Volkhard; Sourjik, Victor; Röth, Volker; Jenal, Urs

doi:10.1016/j.cell.2010.01.018

Cited by 395 publications

(492 citation statements)

References 53 publications

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“…Moreover, CsgD modulates adrA upregulation, which encodes one of the enzymes for cyclic di-GMP synthesis (Ogasawara et al, 2010). c-di-GMP consequently inhibits cell motility by interfering with the flagella motor speed via the c-di-GMP-binding protein YcgR (Wolfe and Visick, 2008;Boehm et al, 2010). From our results, we can suggest that Saci0446 acts in a rather opposite manner when compared with CsgD from E. coli, as Saci0446 activates archaella synthesis and represses genes required for biofilm formation.…”

Section: Regulation Of Crenarchaeal Biofilm Formationmentioning

confidence: 56%

Lrs14 transcriptional regulators influence biofilm formation and cell motility of Crenarchaea

et al. 2013

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Like bacteria, archaea predominately exist as biofilms in nature. However, the environmental cues and the molecular mechanisms driving archaeal biofilm development are not characterized. Here we provide data suggesting that the transcriptional regulators belonging to the Lrs14-like protein family constitute a key regulatory factor during Sulfolobus biofilm development. Among the six lrs14-like genes encoded by Sulfolobus acidocaldarius, the deletion of three led to markedly altered biofilm phenotypes. Although Dsaci1223 and Dsaci1242 deletion mutants were impaired in biofilm formation, the Dsaci0446 deletion strain exhibited a highly increased extracellular polymeric substance (EPS) production, leading to a robust biofilm structure. Moreover, although the expression of the adhesive pili (aap) genes was upregulated, the genes of the motility structure, the archaellum (fla), were downregulated rendering the Dsaci0446 strain non-motile. Gel shift assays confirmed that Saci0446 bound to the promoter regions of fla and aap thus controlling the expression of both cell surface structures. In addition, genetic epistasis analysis using Dsaci0446 as background strain identified a gene cluster involved in the EPS biosynthetic pathway of S. acidocaldarius. These results provide insights into both the molecular mechanisms that govern biofilm formation in Crenarchaea and the functionality of the Lrs14-like proteins, an archaea-specific class of transcriptional regulators.

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Section: Regulation Of Crenarchaeal Biofilm Formationmentioning

confidence: 56%

Lrs14 transcriptional regulators influence biofilm formation and cell motility of Crenarchaea

et al. 2013

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“…The applicability of DRa-CALA to high-throughput metabolite interactomics was demonstrated by screening for binding proteins of an important secondary signaling dinucleotide, cdiGMP. Recent findings have identified cdiGMP as the signaling molecule that controls biofilm formation, motility, and a number of other bacterial functions (2,3,(25)(26)(27). Although the enzymes known to synthesize and degrade cdiGMP are restricted to bacteria, there are questions as to which bacterial species express cdiGMP-binding proteins.…”

Section: Dracala Detection Of Cdigmp-binding Proteins In Diverse Pro-mentioning

confidence: 99%

Differential radial capillary action of ligand assay for high-throughput detection of protein-metabolite interactions

Roelofs

Wang²,

Sintim

et al. 2011

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

177

310

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Interactions of proteins with low-molecular-weight ligands, such as metabolites, cofactors, and allosteric regulators, are important determinants of metabolism, gene regulation, and cellular homeostasis. Pharmaceuticals often target these interactions to interfere with regulatory pathways. We have developed a rapid, precise, and high-throughput method for quantitatively measuring protein-ligand interactions without the need to purify the protein when performed in cells with low background activity. This method, differential radial capillary action of ligand assay (DRaCALA), is based on the ability of dry nitrocellulose to separate the free ligand from bound protein-ligand complexes. Nitrocellulose sequesters proteins and bound ligand at the site of application, whereas free ligand is mobilized by bulk movement of the solvent through capillary action. We show here that DRaCALA allows detection of specific interactions between three nucleotides and their cognate binding proteins. DRaCALA allows quantitative measurement of the dissociation constant and the dissociation rate. Furthermore, DRaCALA can detect the expression of a cyclic-di-GMP (cdiGMP)-binding protein in whole-cell lysates of Escherichia coli, demonstrating the power of the method to bypass the prerequisite for protein purification. We have used DRaCALA to investigate cdiGMP signaling in 54 bacterial species from 37 genera and 7 eukaryotic species. These studies revealed the presence of potential cdiGMP-binding proteins in 21 species of bacteria, including 4 unsequenced species. The ease of obtaining metabolite-protein interaction data using the DRaCALA assay will facilitate rapid identification of protein-metabolite and protein-pharmaceutical interactions in a systematic and comprehensive approach.whole-cell assay I nteractions of low-molecular-weight ligands with protein receptors are critical in biological signaling both between cells and within individual cells. Examples of intercellular signaling mediated by small molecules include quorum signaling in bacteria, hormone and neurotransmitter responses in endocrine systems of animals, and auxin and abscisic acid regulation in plants (1). Intracellular signaling also involves regulatory protein-binding molecules, such as calcium and cyclic nucleotides [e.g., cAMP, cGMP, cyclic-di-GMP (cdiGMP)] (2, 3). In fact, nucleotide receptors are often targets for therapeutic intervention (4). Thus, these protein-small ligand interactions have important implications in modern drug design and use. Considering that many protein-ligand interaction pairs represent potential targets of pharmaceutical intervention in disease or agriculture, there is an urgent need to collect qualitative and quantitative data for such protein-ligand interactions in a highthroughput manner. Current efforts in metabolomics are directed at cataloging the presence of various metabolites through mass spectrometric analysis of biological samples (5-8). However, this approach lacks the ability to confirm interactions with protein partners, and...

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“…The switching probability increases linearly with increase in motor torque in both directions, suggesting that the switch senses the load on the stator-rotor interaction as well as the level of CheY-P (18). Recently, it has been reported that the c-di-GMP binding protein YcgR binds to MotA, FliG, and FliM in the presence of c-di-GMP, resulting not only in a reduced motor speed but also in the CCW bias in motor rotation (3,4). In Rhodobacter sphaeroides, the flagellar motor rotation is unidirectional, but CheY-P acts as a molecular brake to stop motor rotation to change the swimming direction (19).…”

mentioning

confidence: 99%

“…Such behavior is called taxis, which involves sensory reception, signal transduction, and the modulation of the motor function (1). Bacterial motility is also controlled by an intracellular signalling molecule, c-di-GMP, to facilitate biofilm formation, which often causes serious troubles in human life (2)(3)(4). Thus, bacterial motility and behavior are fundamental properties for their life cycle, and hence it is of eminent importance to understand their basic mechanisms for the welfare of human society.…”

mentioning

confidence: 99%

Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor

Nakamura

Kami-ike

Yokota

et al. 2010

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

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The bacterial flagellar motor can rotate in both counterclockwise (CCW) and clockwise (CW) directions. It has been shown that the sodium ion-driven chimeric flagellar motor rotates with 26 steps per revolution, which corresponds to the number of FliG subunits that form part of the rotor ring, but the size of the backward step is smaller than the forward one. Here we report that the protondriven flagellar motor of Salmonella also rotates with 26 steps per revolution but symmetrical in both CCW and CW directions with occasional smaller backward steps in both directions. Occasional shift in the stepping positions is also observed, suggesting the frequent exchange of stators in one of the 11-12 possible anchoring positions around the rotor. These observations indicate that the elementary process of torque generation by the cyclic association/ dissociation of the stator with every FliG subunit along the circumference of the rotor is symmetric in CCW and CW rotation even though the structure of FliG is highly asymmetric and suggests a 180°rotation of a FliG domain for the rotor-stator interaction to reverse the direction of rotation.FliG | MotAB stator complex | Salmonella | stepping rotation | switch

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Second Messenger-Mediated Adjustment of Bacterial Swimming Velocity

Cited by 395 publications

References 53 publications

Lrs14 transcriptional regulators influence biofilm formation and cell motility of Crenarchaea

Lrs14 transcriptional regulators influence biofilm formation and cell motility of Crenarchaea

Differential radial capillary action of ligand assay for high-throughput detection of protein-metabolite interactions

Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor

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