Text S1 Differential affinity and catalytic activity of CheZ in E. coli chemotaxis
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چکیده
The experiments of Vaknin and Berg [1] allow us to verify whether the receptor cluster and the intracellular signaling pathway are indeed two independent modules connected in series. Vaknin and Berg performed experiments on four bacterial strains: wild type CheRCheBCheZ cells, CheR−CheB−CheZ cells lacking CheR and CheB, CheR+CheB+CheZ∗ cells with mutant CheZ proteins that cannot bind the receptor cluster, and CheR−CheB−CheZ∗ cells lacking CheR and CheB and with CheZ∗ (mutated CheZ). As discussed in the main text, we assume that βk0[L] is the same for wild type and CheZ mutant cells, but not for wild type and cheRcheB cells; in contrast, [YpZ](βk0) is the same for wild type and cheRcheB cells, but not for wild type and CheZ mutant cells. If the receptor cluster and the chemotaxis network are two independent modules connected in series, then it should be possible to describe the response curve [YpZ]([L]) of each of the four strains using two of the following response curves: [YpZ] wt(βk0) or [YpZ] ∗(βk0), and βk +B+ 0 ([L]) or βk R−B− 0 ([L]). In other words, all four response curves measured in [1] should be of the compos-
منابع مشابه
Text S2 Differential affinity and catalytic activity of CheZ in E. coli chemotaxis
As dA dt in Eqn. 8 equals zero in steady state, it follows that the steady state of the chemotaxis model with total concentrations [Y]T, [Z]T and [Ap]T is identical to the steady state of a push-pull network with total concentrations [X]T, [Ed]T and [Ea]T, respectively. The remaining concentration of unphosphorylated A is then [A] = [A]T − [Ap]T (Eqn. 12) and βk0 equals k3[ApY][A] (Eqn. 9). Thi...
متن کاملDifferential Affinity and Catalytic Activity of CheZ in E. coli Chemotaxis
Push-pull networks, in which two antagonistic enzymes control the activity of a messenger protein, are ubiquitous in signal transduction pathways. A classical example is the chemotaxis system of the bacterium Escherichia coli, in which the kinase CheA and the phosphatase CheZ regulate the phosphorylation level of the messenger protein CheY. Recent experiments suggest that both the kinase and th...
متن کاملCheZ-mediated dephosphorylation of the Escherichia coli chemotaxis response regulator CheY: role for CheY glutamate 89.
The swimming behavior of Escherichia coli at any moment is dictated by the intracellular concentration of the phosphorylated form of the chemotaxis response regulator CheY, which binds to the base of the flagellar motor. CheY is phosphorylated on Asp57 by the sensor kinase CheA and dephosphorylated by CheZ. Previous work (Silversmith et al., J. Biol. Chem. 276:18478, 2001) demonstrated that rep...
متن کاملAction at a distance: amino acid substitutions that affect binding of the phosphorylated CheY response regulator and catalysis of dephosphorylation can be far from the CheZ phosphatase active site.
Two-component regulatory systems, in which phosphorylation controls the activity of a response regulator protein, provide signal transduction in bacteria. For example, the phosphorylated CheY response regulator (CheYp) controls swimming behavior. In Escherichia coli, the chemotaxis phosphatase CheZ stimulates the dephosphorylation of CheYp. CheYp apparently binds first to the C terminus of CheZ...
متن کاملCobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY
The silent information regulator (Sir2) family proteins are NAD+-dependent deacetylases. Although a few substrates have been identified, functions of the bacteria Sir2-like protein (CobB) still remain unclear. Here the role of CobB on Escherichia coli chemotaxis was investigated. We used Western blotting and mass spectrometry to show that the response regulator CheY is a substrate of CobB. Surf...
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تاریخ انتشار 2009