Potassium Sensing Histidine Kinase in Bacillus subtilis

Methods in Enzymology

Volumn 471, Issue , 2010, Pages 229-251

  López, Daniel ^a   Gontang, Erin A ^a   Kolter, Roberto ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN HISTIDINE KINASE; PROTEIN KINASE; PROTEIN-HISTIDINE KINASE;

ARTICLE; BACILLUS SUBTILIS; BIOFILM; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; PHYSIOLOGY;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; BIOFILMS; GENE EXPRESSION REGULATION, BACTERIAL; PROTEIN KINASES;

MLCS; MLOWN;

EID: 79952198569     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)71013-2     Document Type: Chapter

References (44)

1. Amati, G., Bisicchia, P., Galizzi, A., DegU-P represses expression of the motility fla-che operon in Bacillus subtilis. J. Bacteriol. 186 (2004), 6003–6014.
2. Arima, K., Kakinuma, A., Tamura, G., Surfactin, a crystalline peptidelipid surfactant produced by Bacillus subtilis: Isolation, characterization and its inhibition of fibrin clot formation. Biochem. Biophys. Res. Commun. 31 (1968), 488–494.
3. Bolard, J., How do the polyene macrolide antibiotics affect the cellular membrane properties?. Biochim. Biophys. Acta 864 (1986), 257–304.
4. Branda, S.S., Gonzalez-Pastor, J.E., Ben-Yehuda, S., Losick, R., Kolter, R., Fruiting body formation by Bacillus subtilis. Proc. Natl. Acad. Sci. USA 98 (2001), 11621–11626.
5. Branda, S.S., Gonzalez-Pastor, J.E., Dervyn, E., Ehrlich, S.D., Losick, R., Kolter, R., Genes involved in formation of structured multicellular communities by Bacillus subtilis. J. Bacteriol. 186 (2004), 3970–3979.
6. Branda, S.S., Chu, F., Kearns, D.B., Losick, R., Kolter, R., A major protein component of the Bacillus subtilis biofilm matrix. Mol. Microbiol. 59 (2006), 1229–1238.
7. Butterfield, S.M., Hennig, A., Matile, S., Colorful methods to detect ion channels and pores: Intravesicular chromogenic probes that respond to pH, pM and covalent capture. Org. Biomol. Chem. 7 (2009), 1784–1792.
8. Camilli, A., Bassler, B.L., Bacterial small-molecule signaling pathways. Science 311 (2006), 1113–1116.
9. Chai, Y., Chu, F., Kolter, R., Losick, R., Bistability and biofilm formation in Bacillus subtilis. Mol. Microbiol. 67 (2008), 254–263.
10. Dahl, M.K., Msadek, T., Kunst, F., Rapoport, G., Mutational analysis of the Bacillus subtilis DegU regulator and its phosphorylation by the DegS protein kinase. J. Bacteriol. 173 (1991), 2539–2547.
11. Doan, T., Marquis, K.A., Rudner, D.Z., Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum. Mol. Microbiol. 55 (2005), 1767–1781.
12. Fall, R., Kearns, D.B., Nguyen, T., A defined medium to investigate sliding motility in a Bacillus subtilis flagella-less mutant. BMC Microbiol., 6, 2006, 31.
13. Gu, Y.Z., Hogenesch, J.B., Bradfield, C.A., The PAS superfamily: Sensors of environmental and developmental signals. Annu. Rev. Pharmacol. Toxicol. 40 (2000), 519–561.
14. Hamon, M.A., Lazazzera, B.A., The sporulation transcription factor Spo0A is required for biofilm development in Bacillus subtilis. Mol. Microbiol. 42 (2001), 1199–1209.
15. Hardwood, C.R., Cutting, S.M., Molecular Biological Methods for Bacillus. 1990, Wiley, New York.
16. Hobbs, E.C., Control of cannibalism in Bacillus subtilis. Department of Molecular and Cellular Biology, 2006, Harvard University, Cambridge.
17. Jiang, M., Shao, W., Perego, M., Hoch, J.A., Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis. Mol. Microbiol. 38 (2000), 535–542.
18. Katsu, T., Nakagawa, H., Yasuda, K., Interaction between polyamines and bacterial outer membranes as investigated with ion-selective electrodes. Antimicrob. Agents Chemother. 46 (2002), 1073–1079.
19. Kearns, D.B., Losick, R., Swarming motility in undomesticated Bacillus subtilis. Mol. Microbiol. 49 (2003), 581–590.
20. Kearns, D.B., Losick, R., Cell population heterogeneity during growth of Bacillus subtilis. Genes Dev. 19 (2005), 3083–3094.
21. Kinsinger, R.F., Shirk, M.C., Fall, R., Rapid surface motility in Bacillus subtilis is dependent on extracellular surfactin and potassium ion. J. Bacteriol. 185 (2003), 5627–5631.
22. Kinsinger, R.F., Kearns, D.B., Hale, M., Fall, R., Genetic requirements for potassium ion-dependent colony spreading in Bacillus subtilis. J. Bacteriol. 187 (2005), 8462–8469.
23. Kluge, B., Vater, J., Salnikow, J., Eckart, K., Studies on the biosynthesis of surfactin, a lipopeptide antibiotic from Bacillus subtilis ATCC 21332. FEBS Lett. 231 (1988), 107–110.
24. Kobayashi, K., Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis. Mol. Microbiol. 66 (2007), 395–409.
25. Kobayashi, K., Kuwana, R., Takamatsu, H., kinA mRNA is missing a stop codon in the undomesticated Bacillus subtilis strain ATCC 6051. Microbiology 154 (2008), 54–63.
26. Lauer, P., Chow, M.Y., Loessner, M.J., Portnoy, D.A., Calendar, R., Construction, characterization, and use of two Listeria monocytogenes site-specific phage integration vectors. J. Bacteriol. 184 (2002), 4177–4186.
27. LeDeaux, J.R., Yu, N., Grossman, A.D., Different roles for KinA, KinB, and KinC in the initiation of sporulation in Bacillus subtilis. J. Bacteriol. 177 (1995), 861–863.
28. Lemon, K.P., Higgins, D.E., Kolter, R., Flagellar motility is critical for Listeria monocytogenes biofilm formation. J. Bacteriol. 189 (2007), 4418–4424.
29. Lopez, D., Fischbach, M.A., Chu, F., Losick, R., Kolter, R., Structurally diverse natural products that cause potassium leakage trigger multicellularity in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 106 (2009), 280–285.
30. Lopez, D., Vlamakis, H., Kolter, R., Generation of multiple cell types in Bacillus subtilis. FEMS Microbiol. Rev. 33 (2009), 152–163.
31. Lopez, D., Vlamakis, H., Losick, R., Kolter, R., Paracrine signaling in a bacterium. Genes Dev. 23 (2009), 1631–1638.
32. + by valinomycin in methanol. J. Am. Chem. Soc. 117 (1995), 779–791.
33. Mascher, T., Helmann, J.D., Unden, G., Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol. Mol. Biol. Rev. 70 (2006), 910–938.
34. Ng, W.L., Bassler, B.L., Bacterial quorum-sensing network architectures. Annu. Rev. Genet. 43 (2009), 197–222.
35. Orlov, D.S., Nguyen, T., Lehrer, R.I., Potassium release, a useful tool for studying antimicrobial peptides. J. Microbiol. Methods 49 (2002), 325–328.
36. Sheppard, J.D., Jumarie, C., Cooper, D.G., Laprade, R., Ionic channels induced by surfactin in planar lipid bilayer membranes. Biochim. Biophys. Acta 1064 (1991), 13–23.
37. Smits, W.K., Eschevins, C.C., Susanna, K.A., Bron, S., Kuipers, O.P., Hamoen, L.W., Stripping Bacillus: ComK auto-stimulation is responsible for the bistable response in competence development. Mol. Microbiol. 56 (2005), 604–614.
38. Song, A., Parus, S., Kopelman, R., High-performance fiber-optic pH microsensors for practical physiological measurements using a dual-emission sensitive dye. Anal. Chem. 69 (1997), 863–867.
39. Taylor, B.L., Zhulin, I.B., PAS domains: Internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63 (1999), 479–506.
40. Verhamme, D.T., Kiley, T.B., Stanley-Wall, N.R., DegU co-ordinates multicellular behaviour exhibited by Bacillus subtilis. Mol. Microbiol. 65 (2007), 554–568.
41. Vlamakis, H., Aguilar, C., Losick, R., Kolter, R., Control of cell fate by the formation of an architecturally complex bacterial community. Genes Dev. 22 (2008), 945–953.
42. Wach, A., PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12 (1996), 259–265.
43. Yasbin, R.E., Young, F.E., Transduction in Bacillus subtilis by bacteriophage SPP1. J. Virol. 14 (1974), 1343–1348.
44. Yasuda, K., Ohmizo, C., Katsu, T., Potassium and tetraphenylphosphonium ion-selective electrodes for monitoring changes in the permeability of bacterial outer and cytoplasmic membranes. J. Microbiol. Methods 54 (2003), 111–115.