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. 2022 Nov 5;13:6684. doi: 10.1038/s41467-022-34607-9

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a Bile salts stimulate an increase in intracellular c-di-GMP concentrations. Data were shown as mean ± s.d. of three biological replicates. b Bile salts inhibit the promoter activities of T3SS-1 genes. The promoter activity was determined by quantifying β-galactosidase activity. Data were mean ± s.e.m. of three independent experiments. c Bile salts and the individual bile components taurocholate and taurodeoxycholate stimulate biofilm formation in S. Typhimurium. Data were mean ± s.e.m. of three independent experiments. d Bile-induced enhancement of biofilm formation in S. Typhimurium requires YedQ. Data were presented as mean ± s.e.m. of three independent experiments. e An increase in intracellular c-di-GMP concentrations in response to taurocholate and taurodeoxycholate requires YedQ. Data were mean ± s.d. of three biological replicates. f Taurocholate and taurodeoxycholate bind to the LBD of YedQ with high affinity. ITC data shown are one representative of three independent experiments with similar results. K_d and complex stoichiometry (n) are presented as mean ± s.d. of three independent experiments. g Surface representation of the structural model of YedQ-LBD in complex with taurocholate, prepared using PyMOL. Taurocholate is shown as purple sticks. h Schematic of the predicted contacts between taurocholate and YedQ-LBD from the taurocholate-binding conformation. Potential hydrogen bonds are indicated as green dashed lines. i Binding of taurocholate to YedQ-LBD and its mutants. The binding affinity was measured by ITC. The K_d values are presented as mean ± s.d. of three independent experiments. j Taurocholate and taurodeoxycholate enhance the DGC activity of YedQ in vitro. Data represent mean ± s.e.m. of three independent experiments. K The promoter activities of T3SS-1 genes were inhibited by taurocholate and taurodeoxycholate in the wild-type strain, but not in ΔyedQ. Data were mean ± s.e.m. of three independent experiments. a–e, j, K P values were determined using the two-tailed unpaired Student’s t-test. A p value less than 0.05 was considered to be statistically significant. Source data are provided as a Source Data file.