Journal: microLife

Article Title: The many roles of cyclic di-AMP to control the physiology of Bacillus subtilis

doi: 10.1093/femsml/uqad043

Figure Lengend Snippet: Components of c-di-AMP signaling in B. subtilis . The second messenger c-di-AMP is synthesized by the diadenylate cyclases DisA, CdaA, and CdaS through the condensation of two ATP molecules. Conversely, degradation of c-di-AMP to pApA is facilitated by the phosphodiesterases GdpP and PgpH. C-di-AMP binds to signal transduction proteins that can be regarded as third messengers and can control the expression and activity of several transporters by binding to mRNA riboswitches and proteins, respectively. Red arrows, inhibition; green arrows, activation; gray arrows, regulatory consequences unknown.

Article Snippet: Thus, c-di-AMP-mediated control of KtrAB is exerted mainly at the level of the c-di-AMP-sensitive riboswitch (Rocha et al. ), whereas the constitutively expressed KtrC is the main target for c-di-AMP-mediated control at the protein level (Rocha et al. ).

Techniques: Synthesized, Transduction, Control, Expressing, Activity Assay, Binding Assay, Inhibition, Activation Assay

Journal: microLife

Article Title: The many roles of cyclic di-AMP to control the physiology of Bacillus subtilis

doi: 10.1093/femsml/uqad043

Figure Lengend Snippet: Targets of c-di-AMP in B. subtilis .

Article Snippet: Thus, c-di-AMP-mediated control of KtrAB is exerted mainly at the level of the c-di-AMP-sensitive riboswitch (Rocha et al. ), whereas the constitutively expressed KtrC is the main target for c-di-AMP-mediated control at the protein level (Rocha et al. ).

Techniques: Binding Assay, Inhibition, Activity Assay, Control, Transduction

Journal: Biochemistry

Article Title: Structural and biochemical determinants of ligand binding by the c-di-GMP riboswitch † , ‡

doi: 10.1021/bi100671e

Figure Lengend Snippet: Structures of the G20A/C92U double mutant riboswitch bound to c-di-GMP and c-di-AMP. a. Overlay of the structures of the G20A/C92U mutant riboswitch bound to c-di-GMP and the same RNA bound to c-di-AMP. c-di-GMP is shown in red and c-di-AMP is shown in pink. Binding pocket nucleotides corresponding to the c-di-GMP structure are shown in dark blue and those from the c-di-AMP structure are shown in light blue. b. Overlay of the wild-type structure with the G20A/C92U c-di-AMP bound structure, shown at Aα. c-di-GMP from the wild-type complex is shown in red. c-di-AMP is colored by atom as in Figure 3. G20 from the wild-type structure is shown in dark blue and A20 is colored by atom with oxygen shown in red, nitrogen in blue, and carbon in light blue.. Hydrogen bonds are shown as black dashed lines. c. Overlay of the wild-type structure with the G20A/C92U c-di-AMP bound structure, shown at Aβ. c-di-GMP from the wild-type complex is shown in red. c-di-AMP is colored by atom as in Figure 3. C92 from the wild-type structure is shown in dark blue and U92 is colored by atom with oxygen shown in red, nitrogen in blue, and carbon in light blue. Hydrogen bonds are shown as black dashed lines.

Article Snippet: Both c-di-GMP and c-di-AMP were chemically synthesized on solid support using p-methoxy protected phosphoramidites purchased from ChemGenes ( 24 ).

Techniques: Mutagenesis, Binding Assay