References
- Baer, C.E., Iavarone, A.T., Alber, T., and Sassetti, C.M. (2014). Biochemical and spatial coincidence in the provisional Ser/Thr protein kinase interaction network of Mycobacterium tuberculosis. J. Biol. Chem. 289, 20422-20433. https://doi.org/10.1074/jbc.M114.559054
- Chao, J.D., Papavinasasundaram, K.G., Zheng, X., Chavez-Steenbock, A., Wang, X., Lee, G.Q., and Av-Gay, Y. (2010). Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis. J. Biol. Chem. 285, 29239-29246. https://doi.org/10.1074/jbc.M110.132894
- Chawla, Y., Upadhyay, S., Khan, S., Nagarajan, S.N., Forti, F., and Nandicoori, V.K. (2014). Protein kinase B (PknB) of Mycobacterium tuberculosis is essential for growth of the pathogen in vitro as well as for survival within the host. J. Biol. Chem. 289, 13858-13875. https://doi.org/10.1074/jbc.M114.563536
- Cho, H.Y., Cho, H.J., Kim, Y.M., Oh, J.I., and Kang, B.S. (2009). Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis. J. Biol. Chem. 284, 13057-13067. https://doi.org/10.1074/jbc.M808905200
- Cole, S.T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S.V., Eiglmeier, K., Gas, S., Barry, C.E., 3rd, et al. (1998). Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544. https://doi.org/10.1038/31159
- Fernandez, P., Saint-Joanis, B., Barilone, N., Jackson, M., Gicquel, B., Cole, S.T., and Alzari, P.M. (2006). The Ser/Thr protein kinase PknB is essential for sustaining mycobacterial growth. J. Bacteriol. 188, 7778-7784. https://doi.org/10.1128/JB.00963-06
- Fol, M., Chauhan, A., Nair, N.K., Maloney, E., Moomey, M., Jagannath, C., Madiraju, M.V., and Rajagopalan, M. (2006). Modulation of Mycobacterium tuberculosis proliferation by MtrA, an essential two-component response regulator. Mol. Microbiol. 60, 643-657. https://doi.org/10.1111/j.1365-2958.2006.05137.x
- Fontan, P., Walters, S., and Smith, I. (2004). Cellular signaling pathways and transcriptional regulation in Mycobacterium tuberculosis: stress control and virulence. Curr. Sci. 86, 122-134.
- Fridman, M., Williams, G.D., Muzamal, U., Hunter, H., Siu, K.W., and Golemi-Kotra, D. (2013). Two unique phosphorylation-driven signaling pathways crosstalk in Staphylococcus aureus to modulate the cellwall charge: Stk1/Stp1 meets GraSR. Biochemistry 52, 7975-7986. https://doi.org/10.1021/bi401177n
- Glover, R.T., Kriakov, J., Garforth, S.J., Baughn, A.D., and Jacobs, W.R., Jr. (2007). The two-component regulatory system senX3-regX3 regulates phosphate-dependent gene expression in Mycobacterium smegmatis. J. Bacteriol. 189, 5495-5503. https://doi.org/10.1128/JB.00190-07
- Horstmann, N., Saldana, M., Sahasrabhojane, P., Yao, H., Su, X., Thompson, E., Koller, A., and Shelburne, S.A., 3rd (2014). Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis. PLoS Pathog. 10, e1004088. https://doi.org/10.1371/journal.ppat.1004088
- James, J.N., Hasan, Z.U., Ioerger, T.R., Brown, A.C., Personne, Y., Carroll, P., Ikeh, M., Tilston-Lunel, N.L., Palavecino, C., Sacchettini, J.C., et al. (2012). Deletion of SenX3-RegX3, a key two-component regulatory system of Mycobacterium smegmatis, results in growth defects under phosphate-limiting conditions. Microbiology 158, 2724-2731. https://doi.org/10.1099/mic.0.060319-0
- Jeong, J.A., Baek, E.Y., Kim, S.W., Choi, J.S., and Oh, J.I. (2013). Regulation of the ald gene encoding alanine dehydrogenase by AldR in Mycobacterium smegmatis. J. Bacteriol. 195, 3610-3620. https://doi.org/10.1128/JB.00482-13
- Kang, C.M., Abbott, D.W., Park, S.T., Dascher, C.C., Cantley, L.C., and Husson, R.N. (2005). The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev. 19, 1692-1704. https://doi.org/10.1101/gad.1311105
- Kendall, S.L., Movahedzadeh, F., Rison, S.C., Wernisch, L., Parish, T., Duncan, K., Betts, J.C., and Stoker, N.G. (2004). The Mycobacterium tuberculosis dosRS two-component system is induced by multiple stresses. Tuberculosis (Edinb) 84, 247-255. https://doi.org/10.1016/j.tube.2003.12.007
- Kim, M.J., Park, K.J., Ko, I.J., Kim, Y.M., and Oh, J.I. (2010). Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria. J. Bacteriol. 192, 4868-4875. https://doi.org/10.1128/JB.00550-10
- Kumar, A., Toledo, J.C., Patel, R.P., Lancaster, J.R., Jr., and Steyn, A.J. (2007). Mycobacterium tuberculosis DosS is a redox sensor and DosT is a hypoxia sensor. Proc. Natl. Acad. Sci. U S A 104, 11568-11573. https://doi.org/10.1073/pnas.0705054104
- Laub, M.T., and Goulian, M. (2007). Specificity in two-component signal transduction pathways. Annu. Rev. Genet. 41, 121-145. https://doi.org/10.1146/annurev.genet.41.042007.170548
-
Lee, J.M., Cho, H.Y., Cho, H.J., Ko, I.J., Park, S.W., Baik, H.S., Oh, J.H., Eom, C.Y., Kim, Y.M., Kang, B.S., et al. (2008).
$O_2$ - and NO-sensing mechanism through the DevSR two-component system in Mycobacterium smegmatis. J. Bacteriol. 190, 6795-6804. https://doi.org/10.1128/JB.00401-08 - Lee, H.N., Jung, K.E., Ko, I.J., Baik, H.S., and Oh, J.I. (2012). Proteinprotein interactions between histidine kinases and response regulators of Mycobacterium tuberculosis H37Rv. J. Microbiol. 50, 270-277. https://doi.org/10.1007/s12275-012-2050-4
- Lee, H.N., Lee, N.O., Han, S.J., Ko, I.J., and Oh, J.I. (2014). Regulation of the ahpC gene encoding alkyl hydroperoxide reductase in Mycobacterium smegmatis. PLoS One 9, e111680. https://doi.org/10.1371/journal.pone.0111680
- Leonard, C.J., Aravind, L., and Koonin, E.V. (1998). Novel families of putative protein kinases in bacteria and archaea: evolution of the "eukaryotic" protein kinase superfamily. Genome Res. 8, 1038-1047. https://doi.org/10.1101/gr.8.10.1038
- Lin, W.J., Walthers, D., Connelly, J.E., Burnside, K., Jewell, K.A., Kenney, L.J., and Rajagopal, L. (2009). Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR. Mol. Microbiol. 71, 1477-1495. https://doi.org/10.1111/j.1365-2958.2009.06616.x
- Malhotra, V., Okon, B.P., and Clark-Curtiss, J.E. (2012). Mycobacterium tuberculosis protein kinase K enables growth adaptation through translation control. J. Bacteriol. 194, 4184-4196. https://doi.org/10.1128/JB.00585-12
-
Mayuri, Bagchi, G., Das, T.K., and Tyagi, J.S. (2002). Molecular analysis of the dormancy response in Mycobacterium smegmatis: expression analysis of genes encoding the DevR-DevS twocomponent system, Rv3134c and chaperone
${\alpha}$ -crystallin homologues. FEMS Microbiol. Lett. 211, 231-237. - Menon, S. and Wang, S. (2011). Structure of the response regulator PhoP from Mycobacterium tuberculosis reveals a dimer through the receiver domain. Biochemistry 50, 5948-5957. https://doi.org/10.1021/bi2005575
- Mir, M., Asong, J., Li, X., Cardot, J., Boons, G.J., and Husson, R.N. (2011). The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization. PLoS Pathog. 7, e1002182. https://doi.org/10.1371/journal.ppat.1002182
-
Mouncey, N.J. and Kaplan, S. (1998). Redox-dependent gene regulation in Rhodobacter sphaeroides
$2.4.1^T$ : effects on dimethyl sulfoxide reductase (dor). gene expression. J. Bacteriol. 180, 5612-5618. - Narayan, A., Sachdeva, P., Sharma, K., Saini, A.K., Tyagi, A.K., and Singh, Y. (2007). Serine threonine protein kinases of mycobacterial genus: phylogeny to function. Physiol. Genomics 29, 66-75. https://doi.org/10.1152/physiolgenomics.00221.2006
- Oh, J.I., and Kaplan, S. (1999). The cbb3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: structural and functional implications for the regulation of spectral complex formation. Biochemistry 38, 2688-2696. https://doi.org/10.1021/bi9825100
- Ortega, C., Liao, R., Anderson, L.N., Rustad, T., Ollodart, A.R., Wright, A.T., Sherman, D.R., and Grundner, C. (2014). Mycobacterium tuberculosis Ser/Thr protein kinase B mediates an oxygen-dependent replication switch. PLoS Biol. 12, e1001746. https://doi.org/10.1371/journal.pbio.1001746
- Park, H.D., Guinn, K.M., Harrell, M.I., Liao, R., Voskuil, M.I., Tompa, M., Schoolnik, G.K., and Sherman, D.R. (2003). Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis. Mol. Microbiol. 48, 833-843. https://doi.org/10.1046/j.1365-2958.2003.03474.x
- Pereira, S.F., Goss, L., and Dworkin, J. (2011). Eukaryote-like serine/threonine kinases and phosphatases in bacteria. Microbiol. Mol. Biol. Rev. 75, 192-212. https://doi.org/10.1128/MMBR.00042-10
- Plocinska, R., Purushotham, G., Sarva, K., Vadrevu, I.S., Pandeeti, E.V., Arora, N., Plocinski, P., Madiraju, M.V., and Rajagopalan, M. (2012). Septal localization of the Mycobacterium tuberculosis MtrB sensor kinase promotes MtrA regulon expression. J. Biol. Chem. 287, 23887-23899. https://doi.org/10.1074/jbc.M112.346544
-
Podust, L.M., Ioanoviciu, A., and Ortiz de Montellano, P.R. (2008). 2.3
${\AA}$ X-ray structure of the heme-bound GAF domain of sensory histidine kinase DosT of Mycobacterium tuberculosis. Biochemistry 47, 12523-12531. https://doi.org/10.1021/bi8012356 - Prisic, S., Dankwa, S., Schwartz, D., Chou, M.F., Locasale, J.W., Kang, C.M., Bemis, G., Church, G.M., Steen, H., and Husson, R.N. (2010). Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases. Proc. Natl. Acad. Sci. USA 107, 7521-7526. https://doi.org/10.1073/pnas.0913482107
- Roberts, D.M., Liao, R.P., Wisedchaisri, G., Hol, W.G., and Sherman, D.R. (2004). Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis. J. Biol. Chem. 279, 23082-23087. https://doi.org/10.1074/jbc.M401230200
- Russell, D.G. (2007). Who puts the tubercle in tuberculosis? Nat. Rev. Microbiol. 5, 39-47. https://doi.org/10.1038/nrmicro1538
- Rustad, T.R., Sherrid, A.M., Minch, K.J. and Sherman, D.R. (2009). Hypoxia: a window into Mycobacterium tuberculosis latency. Cell Microbiol. 11, 1151-1159. https://doi.org/10.1111/j.1462-5822.2009.01325.x
- Saini, D.K., Malhotra, V., and Tyagi, J.S. (2004). Cross talk between DevS sensor kinase homologue, Rv2027c, and DevR response regulator of Mycobacterium tuberculosis. FEBS Lett. 565, 75-80. https://doi.org/10.1016/j.febslet.2004.02.092
- Sambrook J, G.M. (2012). Molecular cloning: a laboratory manual, 4th ed. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY).
- Schnappinger, D., Ehrt, S., Voskuil, M.I., Liu, Y., Mangan, J.A., Monahan, I.M., Dolganov, G., Efron, B., Butcher, P.D., Nathan, C., et al. (2003). Transcriptional adaptation of Mycobacterium tuberculosis within Mmrophages: insights into the phagosomal environment. J. Exp. Med. 198, 693-704. https://doi.org/10.1084/jem.20030846
- Shah, I.M., Laaberki, M.H., Popham, D.L., and Dworkin, J. (2008). A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 135, 486-496. https://doi.org/10.1016/j.cell.2008.08.039
-
Sherman, D.R., Voskuil, M., Schnappinger, D., Liao, R., Harrell, M.I., and Schoolnik, G.K. (2001). Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding
${\alpha}$ -crystallin. Proc. Natl. Acad. Sci. U S A 98, 7534-7539. https://doi.org/10.1073/pnas.121172498 - Shi, L., Potts, M., and Kennelly, P.J. (1998). The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: a family portrait. FEMS Microbiol. Rev. 22, 229-253. https://doi.org/10.1111/j.1574-6976.1998.tb00369.x
- Snapper, S.B., Melton, R.E., Mustafa, S., Kieser, T., and Jacobs, W.R., Jr. (1990). Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4, 1911-1919. https://doi.org/10.1111/j.1365-2958.1990.tb02040.x
- Sousa, E.H., Tuckerman, J.R., Gonzalez, G., and Gilles-Gonzalez, M.A. (2007). DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis. Protein Sci. 16, 1708-1719. https://doi.org/10.1110/ps.072897707
- Stock, A.M., Robinson, V.L., and Goudreau, P.N. (2000). Twocomponent signal transduction. Annu. Rev. Biochem. 69, 183-215. https://doi.org/10.1146/annurev.biochem.69.1.183
- Voskuil, M.I., Schnappinger, D., Visconti, K.C., Harrell, M.I., Dolganov, G.M., Sherman, D.R., and Schoolnik, G.K. (2003). Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. J. Exp. Med. 198, 705-713. https://doi.org/10.1084/jem.20030205
- Wayne, L.G. and Sohaskey, C.D. (2001). Nonreplicating persistence of Mycobacterium tuberculosis. Annu. Rev. Microbiol. 55, 139-163. https://doi.org/10.1146/annurev.micro.55.1.139
- Wehenkel, A., Bellinzoni, M., Grana, M., Duran, R., Villarino, A., Fernandez, P., Andre-Leroux, G., England, P., Takiff, H., Cervenansky, C., et al. (2008). Mycobacterial Ser/Thr protein kinases and phosphatases: physiological roles and therapeutic potential. Biochim. Biophys. Acta. 1784, 193-202. https://doi.org/10.1016/j.bbapap.2007.08.006
- West, A.H. and Stock, A.M. (2001). Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26, 369-376. https://doi.org/10.1016/S0968-0004(01)01852-7
- Wisedchaisri, G., Wu, M., Sherman, D.R., and Hol, W.G. (2008). Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation. J. Mol. Biol. 378, 227-242. https://doi.org/10.1016/j.jmb.2008.02.029
-
Yeats, C., Finn, R.D., and Bateman, A. (2002). The PASTA domain:
$a{\beta}$ -lactam-binding domain. Trends Biochem. Sci. 27, 438. https://doi.org/10.1016/S0968-0004(02)02164-3 - Young, T.A., Delagoutte, B., Endrizzi, J.A., Falick, A.M., and Alber, T. (2003). Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. 10, 168-174. https://doi.org/10.1038/nsb897
- Zahrt, T.C. and Deretic, V. (2000). An essential two-component signal transduction system in Mycobacterium tuberculosis. J. Bacteriol. 182, 3832-3838. https://doi.org/10.1128/JB.182.13.3832-3838.2000
Cited by
- Rv2629 Overexpression Delays Mycobacterium smegmatis and Mycobacteria tuberculosis Entry into Log-Phase and Increases Pathogenicity of Mycobacterium smegmatis in Mice vol.8, pp.1664-302X, 2017, https://doi.org/10.3389/fmicb.2017.02231
- vol.293, pp.42, 2018, https://doi.org/10.1074/jbc.RA118.004331
- A Genome-Scale Co-Functional Network of Xanthomonas Genes Can Accurately Reconstruct Regulatory Circuits Controlled by Two-Component Signaling Systems vol.42, pp.2, 2017, https://doi.org/10.14348/molcells.2018.0403
- Dual control of RegX3 transcriptional activity by SenX3 and PknB vol.294, pp.28, 2017, https://doi.org/10.1074/jbc.ra119.008232
- Comparative transcriptomics reveals PrrAB-mediated control of metabolic, respiration, energy-generating, and dormancy pathways in Mycobacterium smegmatis vol.20, pp.1, 2017, https://doi.org/10.1186/s12864-019-6105-3