Methanol production during chemotaxis to amino acids in <i>Bacillus subtilis</i>

Kirby, John R.; Kristich, Christopher J.; Feinberg, Shelby L.; Ordal, George

doi:10.1046/j.1365-2958.1997.3941759.x

Cited by 29 publications

(41 citation statements)

References 36 publications

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“…However, despite this difference in the pattern of methanol release, the ⌬cheR 1 strain was capable of exhibiting normal chemotaxis both on swarm plates and in the tethered cell assay. This is a similar pattern to that observed in wild-type B. subtilis and H. salinarum cells (19,30,47). In B. subtilis the additional proteins CheC and CheD are required for chemoreceptor methylation.…”

Section: Fig 2 Behavior Of Wild-typesupporting

confidence: 67%

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CheR- and CheB-Dependent Chemosensory Adaptation System of Rhodobacter sphaeroides

et al. 2001

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Rhodobacter sphaeroides has multiple homologues of most of the Escherichia coli chemotaxis genes, organized in three major operons and other, unlinked, loci. These include cheA 1 and cheR 1 (che Op 1 ) and cheA 2 , cheR 2 , and cheB 1 (che Op 2 ). In-frame deletions of these cheR and cheB homologues were constructed and the chemosensory behaviour of the resultant mutants examined on swarm plates and in tethered cell assays. Under the conditions tested, CheR 2 and CheB 1 were essential for normal chemotaxis, whereas CheR 1 was not. cheR 2 and cheB 1 , but not cheR 1 , were also able to complement the equivalent E. coli mutants. However, none of the proteins were required for the correct polar localization of the chemoreceptor McpG in R. sphaeroides. In E. coli, CheR binds to the NWETF motif on the high-abundance receptors, allowing methylation of both high-and low-abundance receptors. This motif is not contained on any R. sphaeroides chemoreceptors thus far identified, although 2 of the 13 putative chemoreceptors, McpA and TlpT, do have similar sequences. This suggests that CheR 2 either interacts with the NWETF motif of E. coli methyl-accepting chemotaxis proteins (MCPs), even though its native motif may be slightly different, or with another conserved region of the MCPs. Methanol release measurements show that R. sphaeroides has an adaptation system that is different from that of Bacillus subtilis and E. coli, with methanol release measurable on the addition of attractant but not on its removal. Intriguingly, CheA 2 , but not CheA 1 , is able to phosphorylate CheB 1 , suggesting that signaling through CheA 1 cannot initiate feedback receptor adaptation via CheB 1 -P.

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Section: Fig 2 Behavior Of Wild-typesupporting

confidence: 67%

“…For example, in the grampositive bacterium Bacillus subtilis, CheY-P causes periods of smooth-swimming as opposed to tumbling. In addition, this bacterium shows CheB-dependent methanol release both upon addition and removal of attractant (19,47). Remethylation of the MCPs appears to be dependent on phosphorylated CheY (20).…”

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confidence: 99%

CheR- and CheB-Dependent Chemosensory Adaptation System of Rhodobacter sphaeroides

et al. 2001

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“…Besides the CheC mechanism, there is one that involves methylation/demethylation of the receptors (Hanlon & Ordal, 1994;Kirby et al, 1997;Zimmer et al, 2000Zimmer et al, , 2002 and another that involves phosphorylation of the response regulator CheV (Karatan et al, 2001). We sought to understand how deletion of these adaptational systems affected the unstimulated behaviour of bacteria and their response to attractant.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, the ability of this strain to partially adapt to the addition of asparagine is significant because it suggests that there still exists some measure of post-additional adaptation, despite the lack of all three known adaptation mechanisms: CheR/CheB methylation/demethylation (Hanlon et al, 1993;Kirby et al, 1997;Zimmer et al, 2000Zimmer et al, , 2002, the CheC mechanism (Kirby et al, 2001;Rosario et al, 1995), and CheV phosphorylation (Karatan et al, 2001). It is possible that a fourth (as-yet-unidentified) adaptation mechanism is also present in the chemotaxis system of B. subtilis.…”

Section: Chemotactic Behaviour Generated By Minimal Systemsmentioning

confidence: 99%

Effect of loss of CheC and other adaptational proteins on chemotactic behaviour in Bacillus subtilis

2004

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Bacillus subtilis has a more complex mechanism of chemotaxis than does the paradigm organism, Escherichia coli. In order to understand better the role of the novel chemotaxis proteins -CheC, CheD and CheV -mutants in which increasing numbers of the corresponding genes had been deleted were studied as tethered cells and their biases and sometimes durations of counterclockwise (CCW) and clockwise (CW) flagellar rotations in response to addition and removal of the attractant asparagine were observed. The cheC mutant was found to have considerably reduced switching frequency (that is, prolonged CCW and CW rotations) without a significantly different prestimulus CCW bias, compared with wild-type. This result may indicate that in absence of CheC the switch might be in a conformation less resembling the transition state than in presence of CheC. Conversely, the cheB (methylesterase) mutant showed considerably increased switching frequency without affecting CCW bias, compared with wild-type. Removal of all known adaptation systems -the methylation, CheC and CheV systems -resulted in a mutant (cheRBCDV ) that still retained some adaptation following the addition of attractant.

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“…As with E. coli, Bacillus subtilis possesses a single set of chemotaxis proteins, including CheR and CheB. However, with B. subtilis, methanol is released in response to both the addition and the removal of an attractant (16,34), resulting in a single type of methanol release profile which is different from that of E. coli. Not all chemotactic responses require methylation-dependent adaptation.…”

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confidence: 92%

Role of CheB and CheR in the Complex Chemotactic and Aerotactic Pathway of Azospirillum brasilense

2006

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It has previously been reported that the alpha-proteobacterium Azospirillum brasilense undergoes methylation-independent chemotaxis; however, a recent study revealed cheB and cheR genes in this organism. We have constructed cheB, cheR, and cheBR mutants of A. brasilense and determined that the CheB and CheR proteins under study significantly influence chemotaxis and aerotaxis but are not essential for these behaviors to occur. First, we found that although cells lacking CheB, CheR, or both were no longer capable of responding to the addition of most chemoattractants in a temporal gradient assay, they did show a chemotactic response (albeit reduced) in a spatial gradient assay. Second, in comparison to the wild type, cheB and cheR mutants under steady-state conditions exhibited an altered swimming bias, whereas the cheBR mutant and the che operon mutant did not. Third, cheB and cheR mutants were null for aerotaxis, whereas the cheBR mutant showed reduced aerotaxis. In contrast to the swimming bias for the model organism Escherichia coli, the swimming bias in A. brasilense cells was dependent on the carbon source present and cells released methanol upon addition of some attractants and upon removal of other attractants. In comparison to the wild type, the cheB, cheR, and cheBR mutants showed various altered patterns of methanol release upon exposure to attractants. This study reveals a significant difference between the chemotaxis adaptation system of A. brasilense and that of the model organism E. coli and suggests that multiple chemotaxis systems are present and contribute to chemotaxis and aerotaxis in A. brasilense.

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Methanol production during chemotaxis to amino acids in Bacillus subtilis

Cited by 29 publications

References 36 publications

CheR- and CheB-Dependent Chemosensory Adaptation System of Rhodobacter sphaeroides

CheR- and CheB-Dependent Chemosensory Adaptation System of Rhodobacter sphaeroides

Effect of loss of CheC and other adaptational proteins on chemotactic behaviour in Bacillus subtilis

Role of CheB and CheR in the Complex Chemotactic and Aerotactic Pathway of Azospirillum brasilense

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