Methylation‐independent adaptation in chemotaxis of <i>Escherichia coli</i> involves acetylation‐dependent speed adaptation

Baron, Shoshana; Afanzar, Oshri; Eisenbach, Michael

doi:10.1002/1873-3468.12537

Cited by 4 publications

(4 citation statements)

References 27 publications

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“…All the experiments were carried out at room temperature. The cell tracks were subsequently analyzed for angular velocities by homemade computer software .…”

Section: Methodsmentioning

confidence: 99%

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CheY acetylation is required for ordinary adaptation time in Escherichia coli chemotaxis

Baron

Eisenbach

2017

FEBS Letters

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Recent studies demonstrated the dependence of speed adaptation in Escherichia coli on acetylation of the chemotaxis signaling molecule CheY. Here, we examined whether CheY acetylation is involved in chemotactic adaptation. A mutant lacking the acetylating enzyme acetyl-CoA synthetase (Acs) requires more time to adapt to attractant stimulation, and vice versa to repellent stimulation. This effect is avoided by conditions that favor production of acetyl-CoA, thus enabling Acs-independent CheY autoacetylation, or reversed by expressing Acs from a plasmid. These findings suggest that CheY should be acetylated for ordinary adaptation time, and that the function of this acetylation in adaptation is to enable the motor to shift its rotation to clockwise. We further identify the enzyme phosphotransacetylase as a third deacetylase of CheY in E. coli.

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“…All the experiments were carried out at room temperature. The cell tracks were subsequently analyzed for angular velocities by homemade computer software .…”

Section: Methodsmentioning

confidence: 99%

“…However, methylation‐independent partial adaptation has also been reported . Recently, we demonstrated that methylation‐independent adaptation involves speed adaptation and that this adaptation is dependent on CheY acetylation . This raised the question of whether CheY acetylation is also involved in methylation‐dependent adaptation.…”

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confidence: 94%

CheY acetylation is required for ordinary adaptation time in Escherichia coli chemotaxis

Baron

Eisenbach

2017

FEBS Letters

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“…Several studies in different bacterial species provided preliminary data that taxis systems and flagella can sense protein activities or changes in protein-protein interactions, reviewed in Anderson et al (2010), and also further outlined below. This may be of particular importance for motility functions, since they are required to provide a rapid response to changing environmental conditions, by modifications of either flagellar rotational speed or the direction of rotation (Baron et al, 2017;Koganitsky et al, 2019;Nieto et al, 2019), which are both important for the directionality of the biased random walk. Flagellar speed is set at the rotary motor and its interacting flagellar basal body proteins (Nesper et al, 2017).…”

Section: Modulation Of Motility and Taxis By Co-regulatory Protein-prmentioning

confidence: 99%

Protein Activity Sensing in Bacteria in Regulating Metabolism and Motility

2020

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Bacteria have evolved complex sensing and signaling systems to react to their changing environments, most of which are present in all domains of life. Canonical bacterial sensing and signaling modules, such as membrane-bound ligand-binding receptors and kinases, are very well described. However, there are distinct sensing mechanisms in bacteria that are less studied. For instance, the sensing of internal or external cues can also be mediated by changes in protein conformation, which can either be implicated in enzymatic reactions, transport channel formation or other important cellular functions. These activities can then feed into pathways of characterized kinases, which translocate the information to the DNA or other response units. This type of bacterial sensory activity has previously been termed protein activity sensing. In this review, we highlight the recent findings about this non-canonical sensory mechanism, as well as its involvement in metabolic functions and bacterial motility. Additionally, we explore some of the specific proteins and protein-protein interactions that mediate protein activity sensing and their downstream effects. The complex sensory activities covered in this review are important for bacterial navigation and gene regulation in their dynamic environment, be it host-associated, in microbial communities or free-living.

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“…Furthermore, acetylation cross-talks with other PTMs on CheY. The CheY acetylation is closely related and co-regulated with phosphorylation ( Li et al, 2013), and maybe also associated with methylation-demethylation in chemokinetic adaptation (Baron et al, 2017). The acetylation of CheY is either through nonenzymatic acetylation using AcCoA as the acetyl donor, or through enzymatic acetylation by Acs using AcCoA or acetate.…”

Section: I34 Functional Consequences Of Bacterial Protein Acetylationmentioning

confidence: 99%

Studies of Nε-Lysine Acetylation Modification on Escherichia coli Topoisomerase I

Zhou¹

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Escherichia coli topoisomerase I (TopA), a regulator of global and local DNA supercoiling, is modified by N ε-Lysine acetylation. The sirtuin protein deacetylase CobB can reverse both enzymatic and non-enzymatic lysine acetylation modifications. Here, we explored the effect of lysine acetylation on E. coli topoisomerase I through analysis of TopA relaxation activity and protein expression in cell extract of wild-type and a ΔcobB mutant strains. We showed that the absence of deacetylase CobB in a ΔcobB mutant reduced intracellular TopA relaxation activity while elevating TopA expression and topA gene transcripts levels. Acetyl phosphate mediated lysine acetylation decreased the activity of purified TopA in vitro, and the interaction with purified CobB protected TopA from such inactivation. We explored the physiological significance of TopA acetylation on DNA supercoiling by two-dimensional gel analysis and on cell growth rate by growth curve analysis. We found that the absence of CobB increased negative DNA supercoiling. The vii slow growth phenotype of the ∆cobB mutant can be partially compensated by overexpression of recombinant TopA. In addition, the specific activity of TopA expressed from His-tagged fusion construct in the chromosome was inversely proportional to the degree of in vivo lysine acetylation during growth transition and growth arrest. Investigation of TopA relaxation mechanism using nuclease footprinting and TopA oxidative crosslinking suggested the potential association of TopA acetylation in catalysis. Mass spectrometry analysis of in vitro acetyl phosphate acetylated TopA identified abundant lysine acetylation sites. Substitution of lysine residues by site-directed mutagenesis was used to model the effect of acetylation on individual lysine residues. Our results showed that substitution of Lys-484 with alanine reduced the relaxation activity, suggesting the reduction of TopA relaxation activity by acetylation was probably in part due to acetylation on Lys-484. These findings demonstrate that E. coli topoisomerase I is modulated by lysine acetylation and the prevention of TopA inactivation from excess lysine acetylation and consequent increase in negative DNA supercoiling is an important physiological function of the sirtuin deacetylase CobB. viii

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Methylation‐independent adaptation in chemotaxis of Escherichia coli involves acetylation‐dependent speed adaptation

Cited by 4 publications

References 27 publications

CheY acetylation is required for ordinary adaptation time in Escherichia coli chemotaxis

CheY acetylation is required for ordinary adaptation time in Escherichia coli chemotaxis

Protein Activity Sensing in Bacteria in Regulating Metabolism and Motility

Studies of Nε-Lysine Acetylation Modification on Escherichia coli Topoisomerase I

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