메뉴 건너뛰기




Volumn 192, Issue 17, 2010, Pages 4311-4316

Regulation of galactose metabolism through the HisK:GalR two-component system in Thermoanaerobacter tengcongensis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GALACTOSE; PROTEIN HISTIDINE KINASE; RADIOISOTOPE; REGULATOR PROTEIN; BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; GALACTOSE REPRESSOR PROTEINS; PROTEIN KINASE; PROTEIN-HISTIDINE KINASE; REPRESSOR PROTEIN;

EID: 77956547086     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00402-10     Document Type: Article
Times cited : (6)

References (39)
  • 1
    • 39749140337 scopus 로고    scopus 로고
    • Transcriptional regulation of the Clostridium cellulolyticum cip-cel operon: A complex mechanism involving a catabolite-responsive element
    • Abdou, L., C. Boileau, P. de Philip, S. Pages, H. P. Fierobe, and C. Tardif. 2008. Transcriptional regulation of the Clostridium cellulolyticum cip-cel operon: a complex mechanism involving a catabolite-responsive element. J. Bacteriol. 190:1499-1506.
    • (2008) J. Bacteriol. , vol.190 , pp. 1499-1506
    • Abdou, L.1    Boileau, C.2    De Philip, P.3    Pages, S.4    Fierobe, H.P.5    Tardif, C.6
  • 2
    • 0031795805 scopus 로고    scopus 로고
    • Transcriptional regulation of the Streptococcus mutans gal operon by the GalR repressor
    • Ajdic, D., and J. J. Ferretti. 1998. Transcriptional regulation of the Streptococcus mutans gal operon by the GalR repressor. J. Bacteriol. 180:5727-5732.
    • (1998) J. Bacteriol. , vol.180 , pp. 5727-5732
    • Ajdic, D.1    Ferretti, J.J.2
  • 3
    • 0030597367 scopus 로고    scopus 로고
    • Organization and nucleotide sequence of the Streptococcus mutans galactose operon
    • Ajdic, D., I. C. Sutcliffe, R. R. Russell, and J. J. Ferretti. 1996. Organization and nucleotide sequence of the Streptococcus mutans galactose operon. Gene 180:137-144.
    • (1996) Gene , vol.180 , pp. 137-144
    • Ajdic, D.1    Sutcliffe, I.C.2    Russell, R.R.3    Ferretti, J.J.4
  • 4
    • 0031776947 scopus 로고    scopus 로고
    • The gal genes for the Leloir pathway of Lactobacillus casei 64H
    • Bettenbrock, K., and C. A. Alpert. 1998. The gal genes for the Leloir pathway of Lactobacillus casei 64H. Appl. Environ. Microbiol. 64:2013-2019.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2013-2019
    • Bettenbrock, K.1    Alpert, C.A.2
  • 5
    • 1942517962 scopus 로고    scopus 로고
    • Regulation of virulence determinants in Staphylococcus aureus: Complexity and applications
    • Bronner, S., H. Monteil, and G. Prevost. 2004. Regulation of virulence determinants in Staphylococcus aureus: complexity and applications. FEMS Microbiol. Rev. 28:183-200.
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 183-200
    • Bronner, S.1    Monteil, H.2    Prevost, G.3
  • 6
    • 0025961806 scopus 로고
    • Positive regulation of the pts operon of Escherichia coli: Genetic evidence for a signal transduction mechanism
    • De Reuse, H., and A. Danchin. 1991. Positive regulation of the pts operon of Escherichia coli: genetic evidence for a signal transduction mechanism. J. Bacteriol. 173:727-733.
    • (1991) J. Bacteriol. , vol.173 , pp. 727-733
    • De Reuse, H.1    Danchin, A.2
  • 7
    • 0026808410 scopus 로고
    • Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway
    • Gegner, J. A., D. R. Graham, A. F. Roth, and F. W. Dahlquist. 1992. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell 70:975-982.
    • (1992) Cell , vol.70 , pp. 975-982
    • Gegner, J.A.1    Graham, D.R.2    Roth, A.F.3    Dahlquist, F.W.4
  • 8
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • Gilles-Gonzalez, M. A., G. S. Ditta, and D. R. Helinski. 1991. A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 350:170-172.
    • (1991) Nature , vol.350 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 9
    • 0032514720 scopus 로고    scopus 로고
    • Stabilization of the phospho-aspartyl residue in a two-component signal transduction system in Thermotoga maritima
    • Goudreau, P. N., P. J. Lee, and A. M. Stock. 1998. Stabilization of the phospho-aspartyl residue in a two-component signal transduction system in Thermotoga maritima. Biochemistry 37:14575-14584.
    • (1998) Biochemistry , vol.37 , pp. 14575-14584
    • Goudreau, P.N.1    Lee, P.J.2    Stock, A.M.3
  • 10
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch, J. A. 2000. Two-component and phosphorelay signal transduction. Curr. Opin. Microbiol. 3:165-170.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 12
    • 0027237407 scopus 로고
    • Studies of the hyperthermophile Thermotoga maritima by random sequencing of cDNA and genomic libraries: Identification and sequencing of the trpEG (D) operon
    • Kim, C. W., P. Markiewicz, J. J. Lee, C. F. Schierle, and J. H. Miller. 1993. Studies of the hyperthermophile Thermotoga maritima by random sequencing of cDNA and genomic libraries: identification and sequencing of the trpEG (D) operon. J. Mol. Biol. 231:960-981.
    • (1993) J. Mol. Biol. , vol.231 , pp. 960-981
    • Kim, C.W.1    Markiewicz, P.2    Lee, J.J.3    Schierle, C.F.4    Miller, J.H.5
  • 13
    • 0029819430 scopus 로고    scopus 로고
    • Characterization of the genes and proteins of a two-component system from the hyperthermophilic bacterium Thermotoga maritima
    • Lee, P. J., and A. M. Stock. 1996. Characterization of the genes and proteins of a two-component system from the hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 178:5579-5585.
    • (1996) J. Bacteriol. , vol.178 , pp. 5579-5585
    • Lee, P.J.1    Stock, A.M.2
  • 14
    • 0030942699 scopus 로고    scopus 로고
    • Histidine kinases in signal transduction pathways of eukaryotes
    • Loomis, W. F., G. Shaulsky, and N. Wang. 1997. Histidine kinases in signal transduction pathways of eukaryotes. J. Cell Sci. 110(Pt. 10):1141-1145. (Pubitemid 27254389)
    • (1997) Journal of Cell Science , vol.110 , Issue.10 , pp. 1141-1145
    • Loomis, W.F.1    Shaulsky, G.2    Wang, N.3
  • 15
    • 0015523080 scopus 로고
    • Regulation of the gal operon of Escherichia coli by the capR gene
    • Mackie, G., and D. B. Wilson. 1972. Regulation of the gal operon of Escherichia coli by the capR gene. J. Biol. Chem. 247:2973-2978.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2973-2978
    • Mackie, G.1    Wilson, D.B.2
  • 16
    • 11044228090 scopus 로고    scopus 로고
    • The pmrF polymyxin-resistance operon of Yersinia pseudotuberculosis is upregulated by the PhoP-PhoQ two-component system but not by PmrA-PmrB, and is not required for virulence
    • Marceau, M., F. Sebbane, F. Ewann, F. Collyn, B. Lindner, M. A. Campos, J. A. Bengoechea, and M. Simonet. 2004. The pmrF polymyxin-resistance operon of Yersinia pseudotuberculosis is upregulated by the PhoP-PhoQ two-component system but not by PmrA-PmrB, and is not required for virulence. Microbiology 150:3947-3957.
    • (2004) Microbiology , vol.150 , pp. 3947-3957
    • Marceau, M.1    Sebbane, F.2    Ewann, F.3    Collyn, F.4    Lindner, B.5    Campos, M.A.6    Bengoechea, J.A.7    Simonet, M.8
  • 17
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • Mascher, T., J. D. Helmann, and G. Unden. 2006. Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol. Mol. Biol. Rev. 70:910-938.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 18
    • 33947423948 scopus 로고    scopus 로고
    • The Bacillus subtilis NatK-NatR two-component system regulates expression of the natAB operon encoding an ABC transporter for sodium ion extrusion
    • Ogura, M., K. Tsukahara, K. Hayashi, and T. Tanaka. 2007. The Bacillus subtilis NatK-NatR two-component system regulates expression of the natAB operon encoding an ABC transporter for sodium ion extrusion. Microbiology 153:667-675.
    • (2007) Microbiology , vol.153 , pp. 667-675
    • Ogura, M.1    Tsukahara, K.2    Hayashi, K.3    Tanaka, T.4
  • 19
    • 0030009152 scopus 로고    scopus 로고
    • Adaptive response of the archaeon Sulfolobus acidocaldarius BC65 to phosphate starvation
    • Osorio, G., and C. A. Jerez. 1996. Adaptive response of the archaeon Sulfolobus acidocaldarius BC65 to phosphate starvation. Microbiology 142(Pt. 6):1531-1536.
    • (1996) Microbiology , vol.142 , Issue.PART 6 , pp. 1531-1536
    • Osorio, G.1    Jerez, C.A.2
  • 20
    • 0017328510 scopus 로고
    • Galactose transport in Salmonella typhimurium
    • Postma, P. W. 1977. Galactose transport in Salmonella typhimurium. J. Bacteriol. 129:630-639.
    • (1977) J. Bacteriol. , vol.129 , pp. 630-639
    • Postma, P.W.1
  • 21
    • 0017283184 scopus 로고
    • Involvement of the phosphotransferase system in galactose transport in Salmonella typhimurium
    • Postma, P. W. 1976. Involvement of the phosphotransferase system in galactose transport in Salmonella typhimurium. FEBS Lett. 61:49-53.
    • (1976) FEBS Lett. , vol.61 , pp. 49-53
    • Postma, P.W.1
  • 22
    • 66849093373 scopus 로고    scopus 로고
    • Systematic characterization of a novel gal operon in Thermoanaerobacter tengcongensis
    • Qian, Z., B. Meng, Q. Wang, Z. Wang, C. Zhou, Q. Wang, S. Tu, L. Lin, Y. Ma, and S. Liu. 2009. Systematic characterization of a novel gal operon in Thermoanaerobacter tengcongensis. Microbiology 155:1717-1725.
    • (2009) Microbiology , vol.155 , pp. 1717-1725
    • Qian, Z.1    Meng, B.2    Wang, Q.3    Wang, Z.4    Zhou, C.5    Wang, Q.6    Tu, S.7    Lin, L.8    Ma, Y.9    Liu, S.10
  • 23
    • 0027158879 scopus 로고
    • The MglA component of the binding protein-dependent galactose transport system of Salmonella typhimurium is a galactose-stimulated ATPase
    • Richarme, G., A. el Yaagoubi, and M. Kohiyama. 1993. The MglA component of the binding protein-dependent galactose transport system of Salmonella typhimurium is a galactose-stimulated ATPase. J. Biol. Chem. 268:9473-9477.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9473-9477
    • Richarme, G.1    El Yaagoubi, A.2    Kohiyama, M.3
  • 24
    • 0034025574 scopus 로고    scopus 로고
    • Multiple signals regulate GAL transcription in yeast
    • Rohde, J. R., J. Trinh, and I. Sadowski. 2000. Multiple signals regulate GAL transcription in yeast. Mol. Cell. Biol. 20:3880-3886.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3880-3886
    • Rohde, J.R.1    Trinh, J.2    Sadowski, I.3
  • 25
    • 0037102173 scopus 로고    scopus 로고
    • Operator-bound GalR dimers close DNA loops by direct interaction: Tetramerization and inducer binding
    • Semsey, S., M. Geanacopoulos, D. E. Lewis, and S. Adhya. 2002. Operator-bound GalR dimers close DNA loops by direct interaction: tetramerization and inducer binding. EMBO J. 21:4349-4356.
    • (2002) EMBO J. , vol.21 , pp. 4349-4356
    • Semsey, S.1    Geanacopoulos, M.2    Lewis, D.E.3    Adhya, S.4
  • 27
    • 33646079413 scopus 로고    scopus 로고
    • Three-stage regulation of the amphibolic gal operon: From repressosome to GalR-free DNA
    • Semsey, S., K. Virnik, and S. Adhya. 2006. Three-stage regulation of the amphibolic gal operon: from repressosome to GalR-free DNA. J. Mol. Biol. 358:355-363.
    • (2006) J. Mol. Biol. , vol.358 , pp. 355-363
    • Semsey, S.1    Virnik, K.2    Adhya, S.3
  • 28
    • 34548857623 scopus 로고    scopus 로고
    • Signaling and DNA-binding activities of the Staphylococcus aureus HssR-HssS two-component system required for heme sensing
    • Stauff, D. L., V. J. Torres, and E. P. Skaar. 2007. Signaling and DNA-binding activities of the Staphylococcus aureus HssR-HssS two-component system required for heme sensing. J. Biol. Chem. 282:26111-26121.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26111-26121
    • Stauff, D.L.1    Torres, V.J.2    Skaar, E.P.3
  • 30
    • 0030031939 scopus 로고    scopus 로고
    • Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima
    • Swanson, R. V., M. G. Sanna, and M. I. Simon. 1996. Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 178:484-489.
    • (1996) J. Bacteriol. , vol.178 , pp. 484-489
    • Swanson, R.V.1    Sanna, M.G.2    Simon, M.I.3
  • 31
    • 0019257821 scopus 로고
    • Galactose transport systems in Streptococcus lactis
    • Thompson, J. 1980. Galactose transport systems in Streptococcus lactis. J. Bacteriol. 144:683-691.
    • (1980) J. Bacteriol. , vol.144 , pp. 683-691
    • Thompson, J.1
  • 32
    • 33745884094 scopus 로고    scopus 로고
    • Autoregulation of the MisR/MisS two-component signal transduction system in Neisseria meningitidis
    • Tzeng, Y. L., X. Zhou, S. Bao, S. Zhao, C. Noble, and D. S. Stephens. 2006. Autoregulation of the MisR/MisS two-component signal transduction system in Neisseria meningitidis. J. Bacteriol. 188:5055-5065.
    • (2006) J. Bacteriol. , vol.188 , pp. 5055-5065
    • Tzeng, Y.L.1    Zhou, X.2    Bao, S.3    Zhao, S.4    Noble, C.5    Stephens, D.S.6
  • 33
    • 0036174588 scopus 로고    scopus 로고
    • Galactose and lactose genes from the galactose-positive bacterium Streptococcus salivarius and the phylogenetically related galactose-negative bacterium Streptococcus thermophilus: Organization, sequence, transcription, and activity of the gal gene products
    • Vaillancourt, K., S. Moineau, M. Frenette, C. Lessard, and C. Vadeboncoeur. 2002. Galactose and lactose genes from the galactose-positive bacterium Streptococcus salivarius and the phylogenetically related galactose-negative bacterium Streptococcus thermophilus: organization, sequence, transcription, and activity of the gal gene products. J. Bacteriol. 184:785-793.
    • (2002) J. Bacteriol. , vol.184 , pp. 785-793
    • Vaillancourt, K.1    Moineau, S.2    Frenette, M.3    Lessard, C.4    Vadeboncoeur, C.5
  • 35
    • 0027471001 scopus 로고
    • Control of transcription of gal repressor and isorepressor genes in Escherichia coli
    • Weickert, M. J., and S. Adhya. 1993. Control of transcription of gal repressor and isorepressor genes in Escherichia coli. J. Bacteriol. 175:251-258.
    • (1993) J. Bacteriol. , vol.175 , pp. 251-258
    • Weickert, M.J.1    Adhya, S.2
  • 36
    • 0027429065 scopus 로고
    • The galactose regulon of Escherichia coli
    • Weickert, M. J., and S. Adhya. 1993. The galactose regulon of Escherichia coli. Mol. Microbiol. 10:245-251.
    • (1993) Mol. Microbiol. , vol.10 , pp. 245-251
    • Weickert, M.J.1    Adhya, S.2
  • 37
    • 0015983206 scopus 로고
    • The regulation and properties of the galactose transport system in Escherichia coli K-12
    • Wilson, D. B. 1974. The regulation and properties of the galactose transport system in Escherichia coli K-12. J. Biol. Chem. 249:553-558.
    • (1974) J. Biol. Chem. , vol.249 , pp. 553-558
    • Wilson, D.B.1
  • 38
    • 0034884397 scopus 로고    scopus 로고
    • Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China
    • Xue, Y., Y. Xu, Y. Liu, Y. Ma, and P. Zhou. 2001. Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China. Int. J. Syst. Evol. Microbiol. 51:1335-1341.
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 1335-1341
    • Xue, Y.1    Xu, Y.2    Liu, Y.3    Ma, Y.4    Zhou, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.