메뉴 건너뛰기




Volumn 193, Issue 18, 2011, Pages 4849-4858

The residue threonine 82 of DevR (DosR) is essential for DevR activation and function in Mycobacterium tuberculosis despite its atypical location

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; MUTANT PROTEIN; PROTEIN DEVR; PROTEIN DOSR; REGULATOR PROTEIN; THREONINE; UNCLASSIFIED DRUG;

EID: 80052548122     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05051-11     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0032456891 scopus 로고    scopus 로고
    • Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator activesite quintet
    • Appleby, J. L., and R. B. Bourret. 1998. Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator activesite quintet. J. Bacteriol. 180:3563-3569.
    • (1998) J. Bacteriol. , vol.180 , pp. 3563-3569
    • Appleby, J.L.1    Bourret, R.B.2
  • 2
    • 29244443682 scopus 로고    scopus 로고
    • Transcription and autoregulation of the Rv3134c-devR-devS operon of Mycobacterium tuberculosis
    • Bagchi, G., S. Chauhan, D. Sharma, and J. S. Tyagi. 2005. Transcription and autoregulation of the Rv3134c-devR-devS operon of Mycobacterium tuberculosis. Microbiology 151:4045-4053.
    • (2005) Microbiology , vol.151 , pp. 4045-4053
    • Bagchi, G.1    Chauhan, S.2    Sharma, D.3    Tyagi, J.S.4
  • 3
    • 0029736725 scopus 로고    scopus 로고
    • Structure of the Escherichia coli response regulator NarL
    • Baikalov, I., et al. 1996. Structure of the Escherichia coli response regulator NarL. Biochemistry 35:11053-11061.
    • (1996) Biochemistry , vol.35 , pp. 11053-11061
    • Baikalov, I.1
  • 4
    • 55549111608 scopus 로고    scopus 로고
    • The temporal response of the Mycobacterium tuberculosis gene regulatory network during growth arrest
    • Balazsi, G., A. P. Heath, L. Shi, and M. L. Gennaro. 2008. The temporal response of the Mycobacterium tuberculosis gene regulatory network during growth arrest. Mol. Syst. Biol. 4:225.
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 225
    • Balazsi, G.1    Heath, A.P.2    Shi, L.3    Gennaro, M.L.4
  • 5
    • 0033573063 scopus 로고    scopus 로고
    • Conformational changes induced by phosphorylation of the FixJ receiver domain
    • Birck, C., et al. 1999. Conformational changes induced by phosphorylation of the FixJ receiver domain. Structure 7:1505-1515.
    • (1999) Structure , vol.7 , pp. 1505-1515
    • Birck, C.1
  • 6
    • 77949880884 scopus 로고    scopus 로고
    • Receiver domain structure and function in response regulator proteins
    • Bourret, R. B. 2010. Receiver domain structure and function in response regulator proteins. Curr. Opin. Microbiol. 13:142-149.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 142-149
    • Bourret, R.B.1
  • 7
    • 33644763314 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis cells growing in macrophages are filamentous and deficient in FtsZ rings
    • Chauhan, A., et al. 2006. Mycobacterium tuberculosis cells growing in macrophages are filamentous and deficient in FtsZ rings. J. Bacteriol. 188:1856-1865.
    • (2006) J. Bacteriol. , vol.188 , pp. 1856-1865
    • Chauhan, A.1
  • 8
    • 44949128202 scopus 로고    scopus 로고
    • Cooperative binding of phosphorylated DevR to upstream sites is necessary and sufficient for activation of the Rv3134c-devRS operon in Mycobacterium tuberculosis: implication in the induction of DevR target genes
    • Chauhan, S., and J. S. Tyagi. 2008. Cooperative binding of phosphorylated DevR to upstream sites is necessary and sufficient for activation of the Rv3134c-devRS operon in Mycobacterium tuberculosis: implication in the induction of DevR target genes. J. Bacteriol. 190:4301-4312.
    • (2008) J. Bacteriol. , vol.190 , pp. 4301-4312
    • Chauhan, S.1    Tyagi, J.S.2
  • 9
    • 48149089000 scopus 로고    scopus 로고
    • Interaction of DevR with multiple binding sites synergistically activates divergent transcription of narK2-Rv1738 genes in Mycobacterium tuberculosis
    • Chauhan, S., and J. S. Tyagi. 2008. Interaction of DevR with multiple binding sites synergistically activates divergent transcription of narK2-Rv1738 genes in Mycobacterium tuberculosis. J. Bacteriol. 190:5394-5403.
    • (2008) J. Bacteriol. , vol.190 , pp. 5394-5403
    • Chauhan, S.1    Tyagi, J.S.2
  • 10
    • 70349113557 scopus 로고    scopus 로고
    • Powerful induction of divergent tgs1-Rv3131 genes in Mycobacterium tuberculosis is mediated by DevR interaction with a high-affinity site and an adjacent cryptic low-affinity site
    • Chauhan, S., and J. S. Tyagi. 2009. Powerful induction of divergent tgs1-Rv3131 genes in Mycobacterium tuberculosis is mediated by DevR interaction with a high-affinity site and an adjacent cryptic low-affinity site. J. Bacteriol. 191:6075-6081.
    • (2009) J. Bacteriol. , vol.191 , pp. 6075-6081
    • Chauhan, S.1    Tyagi, J.S.2
  • 11
    • 80052535188 scopus 로고    scopus 로고
    • Comprehensive insights into Mycobacterium tuberculosis DevR (DosR) regulon activation switch
    • 7 June, [Epub ahead of print.] doi: 10.1093/nar/gkr375
    • Chauhan, S., D. Sharma, A. Singh, A. Surolia, and J. S. Tyagi. 7 June 2011. Comprehensive insights into Mycobacterium tuberculosis DevR (DosR) regulon activation switch. Nucleic Acids Res. [Epub ahead of print.] doi: 10.1093/nar/gkr375.
    • (2011) Nucleic Acids Res
    • Chauhan, S.1    Sharma, D.2    Singh, A.3    Surolia, A.4    Tyagi, J.S.5
  • 12
    • 0033802744 scopus 로고    scopus 로고
    • Characterization of a two-component system, devR-devS, of Mycobacterium tuberculosis
    • Dasgupta, N., et al. 2000. Characterization of a two-component system, devR-devS, of Mycobacterium tuberculosis. Tuber. Lung Dis. 80:141-159.
    • (2000) Tuber. Lung Dis. , vol.80 , pp. 141-159
    • Dasgupta, N.1
  • 13
    • 79551548079 scopus 로고    scopus 로고
    • Determinants outside the DevR C-terminal domain are essential for cooperativity and robust activation of dormancy genes in Mycobacterium tuberculosis
    • Gautam, U. S., S. Chauhan, and J. S. Tyagi. 2011. Determinants outside the DevR C-terminal domain are essential for cooperativity and robust activation of dormancy genes in Mycobacterium tuberculosis. PLoS One 6:e16500.
    • (2011) PLoS One , vol.6
    • Gautam, U.S.1    Chauhan, S.2    Tyagi, J.S.3
  • 14
    • 0026499365 scopus 로고
    • The mystery of the mycobacterial 'persistor
    • Grange, J. M. 1992. The mystery of the mycobacterial 'persistor.' Tuber. Lung Dis. 73:249-251.
    • (1992) Tuber. Lung Dis. , vol.73 , pp. 249-251
    • Grange, J.M.1
  • 15
    • 70350048603 scopus 로고    scopus 로고
    • Structurebased design of DevR inhibitor active against nonreplicating Mycobacterium tuberculosis
    • Gupta, R. K., T. S. Thakur, G. R. Desiraju, and J. S. Tyagi. 2009. Structurebased design of DevR inhibitor active against nonreplicating Mycobacterium tuberculosis. J. Med. Chem. 52:6324-6334.
    • (2009) J. Med. Chem. , vol.52 , pp. 6324-6334
    • Gupta, R.K.1    Thakur, T.S.2    Desiraju, G.R.3    Tyagi, J.S.4
  • 17
    • 49649095474 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon
    • Kumar, A., et al. 2008. Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon. J. Biol. Chem. 283: 18032-18039.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18032-18039
    • Kumar, A.1
  • 18
    • 78650994038 scopus 로고    scopus 로고
    • Novel targets in M. tuberculosis: search for new drugs
    • Lamichhane, G. 2010. Novel targets in M. tuberculosis: search for new drugs. Trends Mol. Med. 17:25-33.
    • (2010) Trends Mol. Med. , vol.17 , pp. 25-33
    • Lamichhane, G.1
  • 19
  • 20
    • 62449179440 scopus 로고    scopus 로고
    • Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR
    • Lin, W. J., et al. 2009. Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR. Mol. Microbiol. 71:1477-1495.
    • (2009) Mol. Microbiol. , vol.71 , pp. 1477-1495
    • Lin, W.J.1
  • 21
    • 77949729415 scopus 로고    scopus 로고
    • Expression of DevR and DevR(N)-Aph proteins is associated with hypoxic adaptation defect and virulence attenuation of Mycobacterium tuberculosis
    • Majumdar, S. D., et al. 2010. Expression of DevR and DevR(N)-Aph proteins is associated with hypoxic adaptation defect and virulence attenuation of Mycobacterium tuberculosis. PLoS One 5:e9448.
    • (2010) PLoS One , vol.5
    • Majumdar, S.D.1
  • 22
    • 80052547224 scopus 로고    scopus 로고
    • Ph.D. thesis. All India Institute of Medical Sciences, New Delhi, India
    • Majumdar, S. D., et al. 2010. Ph.D. thesis. All India Institute of Medical Sciences, New Delhi, India.
    • (2010)
    • Majumdar, S.D.1
  • 23
    • 0036786677 scopus 로고    scopus 로고
    • Dimerization allows DNA target site recognition by the NarL response regulator
    • Maris, A. E., et al. 2002. Dimerization allows DNA target site recognition by the NarL response regulator. Nat. Struct. Biol. 9:771-778.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 771-778
    • Maris, A.E.1
  • 24
    • 0036303447 scopus 로고    scopus 로고
    • A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC
    • Mattison, K., R. Oropeza, N. Byers, and L. J. Kenney. 2002. A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC. J. Mol. Biol. 315:497-511.
    • (2002) J. Mol. Biol. , vol.315 , pp. 497-511
    • Mattison, K.1    Oropeza, R.2    Byers, N.3    Kenney, L.J.4
  • 25
    • 24344450314 scopus 로고    scopus 로고
    • An active-like structure in the unphosphorylated StyR response regulator suggests a phosphorylation-dependent allosteric activation mechanism
    • Milani, M., et al. 2005. An active-like structure in the unphosphorylated StyR response regulator suggests a phosphorylation-dependent allosteric activation mechanism. Structure 13:1289-1297.
    • (2005) Structure , vol.13 , pp. 1289-1297
    • Milani, M.1
  • 26
    • 34548152748 scopus 로고    scopus 로고
    • Identification of gene targets against dormant phase Mycobacterium tuberculosis infections
    • Murphy, D. J., and J. R. Brown. 2007. Identification of gene targets against dormant phase Mycobacterium tuberculosis infections. BMC Infect. Dis. 7:84.
    • (2007) BMC Infect. Dis. , vol.7 , pp. 84
    • Murphy, D.J.1    Brown, J.R.2
  • 27
    • 0037371176 scopus 로고    scopus 로고
    • Deletion of two-component regulatory systems increases the virulence of Mycobacterium tuberculosis
    • Parish, T., et al. 2003. Deletion of two-component regulatory systems increases the virulence of Mycobacterium tuberculosis. Infect. Immun. 71: 1134-1140.
    • (2003) Infect. Immun. , vol.71 , pp. 1134-1140
    • Parish, T.1
  • 28
    • 0038349268 scopus 로고    scopus 로고
    • Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis
    • Park, H. D., et al. 2003. Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis. Mol. Microbiol. 48: 833-843.
    • (2003) Mol. Microbiol. , vol.48 , pp. 833-843
    • Park, H.D.1
  • 29
    • 2542475060 scopus 로고    scopus 로고
    • Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis
    • Roberts, D. M., R. P. Liao, G. Wisedchaisri, W. G. Hol, and D. R. Sherman. 2004. Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis. J. Biol. Chem. 279:23082-23087.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23082-23087
    • Roberts, D.M.1    Liao, R.P.2    Wisedchaisri, G.3    Hol, W.G.4    Sherman, D.R.5
  • 30
    • 0033887436 scopus 로고    scopus 로고
    • A tale of two components: a novel kinase and a regulatory switch
    • Robinson, V. L., D. R. Buckler, and A. M. Stock. 2000. A tale of two components: a novel kinase and a regulatory switch. Nat. Struct. Biol. 7:626-633.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 626-633
    • Robinson, V.L.1    Buckler, D.R.2    Stock, A.M.3
  • 31
    • 33947415761 scopus 로고    scopus 로고
    • Identification of mycobacterial sigma factor binding sites by chromatin immunoprecipitation assays
    • Rodrigue, S., et al. 2007. Identification of mycobacterial sigma factor binding sites by chromatin immunoprecipitation assays. J. Bacteriol. 189: 1505-1513.
    • (2007) J. Bacteriol. , vol.189 , pp. 1505-1513
    • Rodrigue, S.1
  • 32
    • 1342292544 scopus 로고    scopus 로고
    • DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR
    • Saini, D. K., et al. 2004. DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR. Microbiology 150:865-875.
    • (2004) Microbiology , vol.150 , pp. 865-875
    • Saini, D.K.1
  • 33
    • 2342661639 scopus 로고    scopus 로고
    • Cross talk between DevS sensor kinase homologue, Rv2027c, and DevR response regulator of Mycobacterium tuberculosis
    • Saini, D. K., V. Malhotra, and J. S. Tyagi. 2004. Cross talk between DevS sensor kinase homologue, Rv2027c, and DevR response regulator of Mycobacterium tuberculosis. FEBS Lett. 565:75-80.
    • (2004) FEBS Lett , vol.565 , pp. 75-80
    • Saini, D.K.1    Malhotra, V.2    Tyagi, J.S.3
  • 34
    • 0035912791 scopus 로고    scopus 로고
    • Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha-crystallin
    • Sherman, D. R., et al. 2001. Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha-crystallin. Proc. Natl. Acad. Sci. U. S. A. 98:7534-7539.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7534-7539
    • Sherman, D.R.1
  • 35
    • 43049170080 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection
    • Shiloh, M. U., P. Manzanillo, and J. S. Cox. 2008. Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection. Cell Host Microbe 3:323-330.
    • (2008) Cell Host Microbe , vol.3 , pp. 323-330
    • Shiloh, M.U.1    Manzanillo, P.2    Cox, J.S.3
  • 36
    • 0014082851 scopus 로고
    • Pathogenesis of a first episode of chronic pulmonary tuberculosis in man: recrudescence of residuals of the primary infection or exogenous reinfection?
    • Stead, W. W. 1967. Pathogenesis of a first episode of chronic pulmonary tuberculosis in man: recrudescence of residuals of the primary infection or exogenous reinfection? Am. Rev. Respir. Dis. 95:729-745.
    • (1967) Am. Rev. Respir. Dis. , vol.95 , pp. 729-745
    • Stead, W.W.1
  • 38
    • 77956277547 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis transcriptional adaptation, growth arrest and dormancy phenotype development is triggered by vitamin C
    • Taneja, N. K., S. Dhingra, A. Mittal, M. Naresh, and J. S. Tyagi. 2010. Mycobacterium tuberculosis transcriptional adaptation, growth arrest and dormancy phenotype development is triggered by vitamin C. PLoS One 5:e10860.
    • (2010) PLoS One , vol.5
    • Taneja, N.K.1    Dhingra, S.2    Mittal, A.3    Naresh, M.4    Tyagi, J.S.5
  • 39
    • 0030003134 scopus 로고    scopus 로고
    • Applications for green fluorescent protein (GFP) in the study of host-pathogen interactions
    • Valdivia, R. H., A. E. Hromockyj, D. Monack, L. Ramakrishnan, and S. Falkow. 1996. Applications for green fluorescent protein (GFP) in the study of host-pathogen interactions. Gene 173:47-52.
    • (1996) Gene , vol.173 , pp. 47-52
    • Valdivia, R.H.1    Hromockyj, A.E.2    Monack, D.3    Ramakrishnan, L.4    Falkow, S.5
  • 41
    • 0042140672 scopus 로고    scopus 로고
    • Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program
    • Voskuil, M. I., et al. 2003. Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. J. Exp. Med. 198:705-713.
    • (2003) J. Exp. Med. , vol.198 , pp. 705-713
    • Voskuil, M.I.1
  • 42
    • 0029976980 scopus 로고    scopus 로고
    • An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence
    • Wayne, L. G., and L. G. Hayes. 1996. An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence. Infect. Immun. 64:2062-2069.
    • (1996) Infect. Immun. , vol.64 , pp. 2062-2069
    • Wayne, L.G.1    Hayes, L.G.2
  • 43
    • 0034780485 scopus 로고    scopus 로고
    • Nonreplicating persistence of mycobacterium tuberculosis
    • Wayne, L. G., and C. D. Sohaskey. 2001. Nonreplicating persistence of mycobacterium tuberculosis. Annu. Rev. Microbiol. 55:139-163.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 139-163
    • Wayne, L.G.1    Sohaskey, C.D.2
  • 44
    • 0026783517 scopus 로고
    • Isolation of phosphorylation-deficient mutants of the Rhizobium meliloti two-component regulatory protein
    • Weinstein, M., A. F. Lois, E. K. Monson, G. S. Ditta, and D. R. Helinski. 1992. Isolation of phosphorylation-deficient mutants of the Rhizobium meliloti two-component regulatory protein, FixJ. Mol. Microbiol. 6:2041-2049.
    • (1992) FixJ. Mol. Microbiol. , vol.6 , pp. 2041-2049
    • Weinstein, M.1    Lois, A.F.2    Monson, E.K.3    Ditta, G.S.4    Helinski, D.R.5
  • 45
    • 41149103311 scopus 로고    scopus 로고
    • Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation
    • Wisedchaisri, G., M. Wu, D. R. Sherman, and W. G. Hol. 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.
    • (2008) J. Mol. Biol. , vol.378 , pp. 227-242
    • Wisedchaisri, G.1    Wu, M.2    Sherman, D.R.3    Hol, W.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.