<i>Bacillus subtilis</i> chemotaxis: a deviation from the <i>Escherichia coli</i> paradigm

Bischoff, David S.; Ordal, George

doi:10.1111/j.1365-2958.1992.tb00833.x

Cited by 88 publications

(67 citation statements)

References 28 publications

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“…A feasible information exchange may be based upon a chemotaxis-dependent methyl transfer that would occur at a rate much slower than in chemotaxis. It could be hypothesized that Ordal's intermediate methyl acceptor X [2] might serve as an integrating site transmitting chemotactic sensory input from MCPs to the sporulation triggering mechanisms. Slow changes in the methylation state of X during the culture growth would represent an integrated signal for nutrients presence or depletion in the environment.…”

Section: S-adenosyhnethioninementioning

confidence: 99%

“…SAM is a donor of a methyl group for the methylation of MCPs in B. subtilis [2,4] as well. In contrast to E. coZi and S. typhimurium, this bacterium can convert L-ethionine into S-adenosylethionine [16].…”

Section: S-adenosyhnethioninementioning

confidence: 99%

“…Although all key components of the enterobacterial chemotactic system are conserved in Bacilli [2], the methyl group is not removed from MCPs to water but is transferred to an intermediate methyl acceptor termed by Ordal 'X' [2,11]. The function of this protein is unknown.…”

Section: Introductionmentioning

confidence: 99%

“…The biochemical nature of the system registering nutrient depletion and generating primary signals for the initiation of sporulation is unknown. The system responsive to the fluctuation of temporary nutrient gradient, namely, the chemotactic system has been studied in detail [2]. It was suggested by Sherman [3] that the chemotaxis system may gather the information concerning nutrient concentrations and transmit signals to sporulation control mechanisms.…”

Section: Introductionmentioning

confidence: 99%

“…Protein transmethylation seems to be a shared regulation principle for both regulatory systems [2,5,6]. In B. subtilis [7,8] as well as in B. sphaericus [9], attractants cause a transient increase in the methyl group turnover on methyl-accepting chemotaxis proteins (MCPs).…”

Section: Introductionmentioning

confidence: 99%

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Chemotaxis, sporulation, and larvicide production in Bacillus sphaericus 2362

et al. 1994

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CAminophenylboronic acid (APBA), a known inhibitor of sporulation in Bacilli, as well as L-ethionine, a known inhibitor of chemotaxis in Enterobacteria, inhibited both sporulation and chemotactic behavior but not growth of BaciZZus sphaericus. Both compounds also inhibited the methyl group turnover on the methyl-accepting chemotaxis protein (P53) in this microorganism. Sporulation of B. spbaericus was inhibited only when APBA was added to the growing culture before the late logarithmic stage. It was previously demonstrated that the ability of B. sphuericus to respond to chemoattractants sharply declines at the same age of the culture. Thus, it seems plausible that the action of both inhibitors upon sporulation may be attributed to the inhibition of some regulatory pathway common to chemotaxis and sporulation and involving protein methylation. Possible exchange of the nutrient depletion-related sensory information between chemotaxis and sporulation systems at the level of methyl group transfer is discussed.

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Section: S-adenosyhnethioninementioning

confidence: 99%

Section: S-adenosyhnethioninementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Chemotaxis, sporulation, and larvicide production in Bacillus sphaericus 2362

et al. 1994

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Phosphorylation in halobacterial signal transduction.

et al. 1995

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Regulated phosphorylation of proteins has been shown to be a hallmark of signal transduction mechanisms in both Eubacteria and Eukarya. Here we demonstrate that phosphorylation and dephosphorylation are also the underlying mechanism of chemo‐ and phototactic signal transduction in Archaea, the third branch of the living world. Cloning and sequencing of the region upstream of the cheA gene, known to be required for chemo‐ and phototaxis in Halobacterium salinarium, has identified cheY and cheB analogs which appear to form part of an operon which also includes cheA and the following open reading frame of 585 nucleotides. The CheY and CheB proteins have 31.3 and 37.5% sequence identity compared with the known signal transduction proteins CheY and CheB from Escherichia coli, respectively. The biochemical activities of both CheA and CheY were investigated following their expression in E.coli, isolation and renaturation. Wild‐type CheA could be phosphorylated in a time‐dependent manner in the presence of [gamma‐32P]ATP and Mg2+, whereas the mutant CheA(H44Q) remained unlabeled. Phosphorylated CheA was dephosphorylated rapidly by the addition of wild‐type CheY. The mutant CheY(D53A) had no effect on phosphorylated CheA. The mechanism of chemo‐ and phototactic signal transduction in the Archaeon H.salinarium, therefore, is similar to the two‐component signaling system known from chemotaxis in the eubacterium E.coli.

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Resonance Raman studies of gas sensing heme proteins

Liu

Kincaid

2021

J Raman Spectroscopy

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Heme sensor proteins are present in organisms ranging from bacteria to mammals, typically consisting of a catalytic domain and a heme-containing sensor domain, which can bind diatomic gas molecules such as O 2 , CO, and NO. Such ligand binding event can induce active site conformational changes that are subsequently propagated to the functional domain, ultimately activating/deactivating a series of biological events, such as aerotaxis, gene expression, changes the metabolic pathway, and so forth. Such regulatory events are crucial for the cell to fulfill the physiological functions by regulating enzyme activity in response to the external stimuli. Resonance Raman (rR) spectroscopy is an effective method to investigate the sensing mechanism of these structurally different associated sensor proteins that exhibit diverse inherent physiological functions. This review summarizes the results of rR studies on a diverse collection of these heme sensor proteins, including FixL, Escherichia coli direct oxygen sensor (EcDOS), HemAT from Bacillus subtilis (HemAT-Bs), CooA, soluble guanylyl cyclase (sGC), heme nitric oxide and/or oxygen binding domain (H-NOX), and nitric oxide sensing proteins (NosP).

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Bacillus subtilis chemotaxis: a deviation from the Escherichia coli paradigm

Cited by 88 publications

References 28 publications

Chemotaxis, sporulation, and larvicide production in Bacillus sphaericus 2362

Chemotaxis, sporulation, and larvicide production in Bacillus sphaericus 2362

Phosphorylation in halobacterial signal transduction.

Resonance Raman studies of gas sensing heme proteins

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