Response regulator output in bacterial chemotaxis
Identifieur interne : 002905 ( Istex/Curation ); précédent : 002904; suivant : 002906Response regulator output in bacterial chemotaxis
Auteurs : Uri Alon [États-Unis] ; Laura Camarena [Mexique] ; Michael G. Surette [Canada] ; Blaise Aguera Y Arcas [États-Unis] ; Yi Liu [États-Unis] ; Stanislas Leibler [États-Unis] ; Jeffry B. Stock [États-Unis]Source :
- The EMBO Journal [ 0261-4189 ] ; 1998-08-03.
Abstract
Chemotaxis responses in Escherichia coli are mediated by the phosphorylated response‐regulator protein P‐CheY. Biochemical and genetic studies have established the mechanisms by which the various components of the chemotaxis system, the membrane receptors and Che proteins function to modulate levels of CheY phosphorylation. Detailed models have been formulated to explain chemotaxis sensing in quantitative terms; however, the models cannot be adequately tested without knowledge of the quantitative relationship between P‐CheY and bacterial swimming behavior. A computerized image analysis system was developed to collect extensive statistics on freeswimming and individual tethered cells. P‐CheY levels were systematically varied by controlled expression of CheY in an E.coli strain lacking the CheY phosphatase, CheZ, and the receptor demethylating enzyme CheB. Tumbling frequency was found to vary with P‐CheY concentration in a weakly sigmoidal fashion (apparent Hill coefficient ∼2.5). This indicates that the high sensitivity of the chemotaxis system is not derived from highly cooperative interactions between P‐CheY and the flagellar motor, but rather depends on nonlinear effects within the chemotaxis signal transduction network. The complex relationship between single flagella rotation and free‐swimming behavior was examined; our results indicate that there is an additional level of information processing associated with interactions between the individual flagella. An allosteric model of the motor switching process is proposed which gives a good fit to the observed switching induced by P‐CheY. Thus the level of intracellular P‐CheY can be estimated from behavior determinations: ∼30% of the intracellular pool of CheY appears to be phosphorylated in fully adapted wild‐type cells.
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DOI: 10.1093/emboj/17.15.4238
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Surette</name><affiliation wicri:level="1"><mods:affiliation>Department of Microbiology and Infectious Diseases, University of Calgary, AB, T2N 4N1, Calgary, Canada</mods:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Microbiology and Infectious Diseases, University of Calgary, AB, T2N 4N1, Calgary</wicri:regionArea></affiliation></author><author><name sortKey="Aguera Y Arcas, Blaise" sort="Aguera Y Arcas, Blaise" uniqKey="Aguera Y Arcas B" first="Blaise" last="Aguera Y Arcas">Blaise Aguera Y Arcas</name><affiliation wicri:level="1"><mods:affiliation>Department of Molecular Biology, Princeton University, NJ, 08544, Princeton, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology, Princeton University, NJ, 08544, Princeton</wicri:regionArea></affiliation></author><author><name sortKey="Liu, Yi" sort="Liu, Yi" uniqKey="Liu Y" first="Yi" last="Liu">Yi Liu</name><affiliation wicri:level="1"><mods:affiliation>Department of Molecular Biology, Princeton University, NJ, 08544, Princeton, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology, Princeton University, NJ, 08544, Princeton</wicri:regionArea></affiliation></author><author><name sortKey="Leibler, Stanislas" sort="Leibler, Stanislas" uniqKey="Leibler S" first="Stanislas" last="Leibler">Stanislas Leibler</name><affiliation wicri:level="1"><mods:affiliation>Department of Molecular Biology, Princeton University, 08544, Princeton, NJ, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology, Princeton University, 08544, Princeton, NJ</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Department of Physics, Princeton University, NJ, 08544, Princeton, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics, Princeton University, NJ, 08544, Princeton</wicri:regionArea></affiliation></author><author><name sortKey="Stock, Jeffry B" sort="Stock, Jeffry B" uniqKey="Stock J" first="Jeffry B." last="Stock">Jeffry B. Stock</name><affiliation wicri:level="1"><mods:affiliation>Department of Molecular Biology, Princeton University, 08544, Princeton, NJ, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology, Princeton University, 08544, Princeton, NJ</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Department of Chemistry, Princeton University, NJ, 08544, Princeton, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Princeton University, NJ, 08544, Princeton</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">The EMBO Journal</title><idno type="ISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><imprint><publisher>John Wiley & Sons, Ltd</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="1998-08-03">1998-08-03</date><biblScope unit="volume">17</biblScope><biblScope unit="issue">15</biblScope><biblScope unit="page" from="4238">4238</biblScope><biblScope unit="page" to="4248">4248</biblScope></imprint><idno type="ISSN">0261-4189</idno></series><idno type="istex">7C8253C0963DD271F50D268ABA862C84F957DA4C</idno><idno type="DOI">10.1093/emboj/17.15.4238</idno><idno type="ArticleID">EMBJ7591124</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0261-4189</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">Chemotaxis responses in Escherichia coli are mediated by the phosphorylated response‐regulator protein P‐CheY. Biochemical and genetic studies have established the mechanisms by which the various components of the chemotaxis system, the membrane receptors and Che proteins function to modulate levels of CheY phosphorylation. Detailed models have been formulated to explain chemotaxis sensing in quantitative terms; however, the models cannot be adequately tested without knowledge of the quantitative relationship between P‐CheY and bacterial swimming behavior. A computerized image analysis system was developed to collect extensive statistics on freeswimming and individual tethered cells. P‐CheY levels were systematically varied by controlled expression of CheY in an E.coli strain lacking the CheY phosphatase, CheZ, and the receptor demethylating enzyme CheB. Tumbling frequency was found to vary with P‐CheY concentration in a weakly sigmoidal fashion (apparent Hill coefficient ∼2.5). This indicates that the high sensitivity of the chemotaxis system is not derived from highly cooperative interactions between P‐CheY and the flagellar motor, but rather depends on nonlinear effects within the chemotaxis signal transduction network. The complex relationship between single flagella rotation and free‐swimming behavior was examined; our results indicate that there is an additional level of information processing associated with interactions between the individual flagella. An allosteric model of the motor switching process is proposed which gives a good fit to the observed switching induced by P‐CheY. Thus the level of intracellular P‐CheY can be estimated from behavior determinations: ∼30% of the intracellular pool of CheY appears to be phosphorylated in fully adapted wild‐type cells.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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