The Bacillus subtilis Chemoreceptor McpC Senses Multiple Ligands Using Two Discrete Mechanisms

Glekas, George D.; Mulhern, Brendan J.; Kroc, Abigail; Duelfer, Keegan A.; Lei, Victor; Rao, Christopher V.; Ordal, George

doi:10.1074/jbc.m112.413518

Cited by 76 publications

(96 citation statements)

References 28 publications

(29 reference statements)

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“…Relative strength of attraction was not related to the aa class, with arg, phe, pro, and trp as the strongest attractants being positively charged and hydrophobic, respectively. A comparable lack of correlation was reported for aa taxis in Escherichia coli and Bacillus subtilis (Glekas et al 2012;Mesibov and Adler 1972). No clear relationship was seen between the strength of attraction and the amount exuded by germinating alfalfa seeds (Webb et al 2016).…”

Section: Discussionmentioning

confidence: 87%

“…The prediction was supported by chemotaxis behavioral assays of single point mutants and in vitro binding analysis of purified mutant variant proteins (Webb et al 2014). The recognized motif, also known as a double PhoQ-DcuS-CitA (PDC) domain, recognizes aa directly as well as indirectly through ABC transport-binding lipoproteins (Anantharaman and Aravind 2000;Glekas et al 2012;McKellar et al 2015;Reyes-Darias et al 2015;Ulrich and Zhulin 2005;Webb et al 2014).…”

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confidence: 97%

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Sinorhizobium meliloti Chemotaxis to Multiple Amino Acids Is Mediated by the Chemoreceptor McpU

Webb

Compton

Campo

et al. 2017

MPMI

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The legume symbiont Sinorhizobium meliloti is chemoattracted to compounds exuded by germinating seeds of its host alfalfa. This response is mainly mediated by the S. meliloti chemoreceptor McpU. McpU also has a prominent contribution in sensing a synthetic amino acid (aa) mixture mimicking the amounts and composition observed in seed exudate. Here, we used the hydrogel capillary assay to quantify chemotactic responses of S. meliloti to individual aa exuded by germinating alfalfa seeds and to define the role of McpU in this behavior. S. meliloti exhibited positive chemotaxis responses to all proteinogenic aa, except for aspartate, and to citrulline, cystine, gamma-aminobutyric acid, and ornithine. Wild-type responses were diverse in intensity, while a strain lacking mcpU displayed strongly diminished responses. Differential scanning fluorimetry demonstrated interaction of the purified periplasmic region of McpU (McpU-PR) with the aa, except glutamate and aspartate. We additionally tested organic acids and sugars, but there were no significant interactions with the McpU ligand-binding domain, except for citrate. Using ligand displacement, we confirmed the interaction of McpU-PR with aa representing strong and weak attractants. Our results show that S. meliloti McpU is a broad-range aa receptor mediating differential responses to individual attractants, which does not bind negatively charged aa.

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Section: Discussionmentioning

confidence: 87%

mentioning

confidence: 97%

Sinorhizobium meliloti Chemotaxis to Multiple Amino Acids Is Mediated by the Chemoreceptor McpU

Webb

Compton

Campo

et al. 2017

MPMI

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“…This suggests that a subset of the chemotactic community is made of 'generalist chemotaxers' that have the capacity to sense and direct movement in response to diverse chemicals compounds. Currently, little is known about the chemoreceptors used by marine bacteria (Stocker and Seymour, 2012), but the generalist chemotaxers identified here may either have multiple sets of chemoreceptors, which allow them to respond to a variety of compounds (Wadhams and Armitage, 2004;Parales et al, 2013), or single chemoreceptors that allow for binding of multiple compounds (Adler, 1969;Glekas et al, 2012). However, the bulk (76.4%) of chemotactic OTUs identified here can be classified as 'specialist chemotaxers', as they responded to only one compound.…”

Section: Sandy Substratementioning

confidence: 84%

Chemotaxis by natural populations of coral reef bacteria

et al. 2015

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Corals experience intimate associations with distinct populations of marine microorganisms, but the microbial behaviours underpinning these relationships are poorly understood. There is evidence that chemotaxis is pivotal to the infection process of corals by pathogenic bacteria, but this evidence is limited to experiments using cultured isolates under laboratory conditions. We measured the chemotactic capabilities of natural populations of coral-associated bacteria towards chemicals released by corals and their symbionts, including amino acids, carbohydrates, ammonium and dimethylsulfoniopropionate (DMSP). Laboratory experiments, using a modified capillary assay, and in situ measurements, using a novel microfabricated in situ chemotaxis assay, were employed to quantify the chemotactic responses of natural microbial assemblages on the Great Barrier Reef. Both approaches showed that bacteria associated with the surface of the coral species Pocillopora damicornis and Acropora aspera exhibited significant levels of chemotaxis, particularly towards DMSP and amino acids, and that these levels of chemotaxis were significantly higher than that of bacteria inhabiting nearby, non-coral-associated waters. This pattern was supported by a significantly higher abundance of chemotaxis and motility genes in metagenomes within coral-associated water types. The phylogenetic composition of the coral-associated chemotactic microorganisms, determined using 16S rRNA amplicon pyrosequencing, differed from the community in the seawater surrounding the coral and comprised known coral associates, including potentially pathogenic Vibrio species. These findings indicate that motility and chemotaxis are prevalent phenotypes among coral-associated bacteria, and we propose that chemotaxis has an important role in the establishment and maintenance of specific coral-microbe associations, which may ultimately influence the health and stability of the coral holobiont.

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“…The following rotation angles were observed: 171.6 and 172. 4 in 3E4P and 3E4Q (DctB 29,30 ), 174.4 in KinD-SD (this work), 176.2 in 3C8C, 32 179.2 in 3T4J 34 and 180 in 3LIA, 3LI8, and 3LI9. 31 In 3LI8…”

Section: Comparison Of Periplasmic Sensors Composed Of Tandem Pas-likmentioning

confidence: 99%

“…As mentioned above, the chemotaxis sensor, McpC, binds and responds to 11 amino acids directly, adding to the dual PAS-like sensors that respond to multiple ligands. 29 …”

Section: Is Pyruvate the Physiological Ligand Of Kind?mentioning

confidence: 99%

Insight into the sporulation phosphorelay: Crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD

Wilton

et al. 2013

Protein Science

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The Bacillus subtilis KinD signal-transducing histidine kinase is a part of the sporulation phosphorelay known to regulate important developmental decisions such as sporulation and biofilm formation. We have determined crystal structures of the extracytoplasmic sensing domain of KinD, which was copurified and crystallized with a pyruvate ligand. The structure of a ligandbinding site mutant was also determined; it was copurified and crystallized with an acetate ligand. The structure of the KinD extracytoplasmic segment is similar to that of several other sensing domains of signal transduction proteins and is composed of tandem Per-Arnt-Sim (PAS)-like domains. The KinD ligand-binding site is located on the membrane distal PAS-like domain and appears to be highly selective; a single mutation, R131A, abolishes pyruvate binding and the mutant binds acetate instead. Differential scanning fluorimetry, using a variety of monocarboxylic and dicarboxylic acids, identified pyruvate, propionate, and butyrate but not lactate, acetate, or malate as KinD ligands. A recent report found that malate induces biofilm formation in a KinDdependent manner. It was suggested that malate might induce a metabolic shift and increased secretion of the KinD ligand of unknown identity. The structure and binding assays now suggests that this ligand is pyruvate and/or other small monocarboxylic acids. In summary, this study gives a first insight into the identity of a molecular ligand for one of the five phosphorelay kinases of B. subtilis.

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The Bacillus subtilis Chemoreceptor McpC Senses Multiple Ligands Using Two Discrete Mechanisms

Cited by 76 publications

References 28 publications

Sinorhizobium meliloti Chemotaxis to Multiple Amino Acids Is Mediated by the Chemoreceptor McpU

Sinorhizobium meliloti Chemotaxis to Multiple Amino Acids Is Mediated by the Chemoreceptor McpU

Chemotaxis by natural populations of coral reef bacteria

Insight into the sporulation phosphorelay: Crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD

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