메뉴 건너뛰기




Volumn 186, Issue 6, 2004, Pages 1694-1704

Mutational Analysis of the Signal-Sensing Domain of ResE Histidine Kinase from Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

NITRATE; NITRIC OXIDE; PROTEIN HISTIDINE KINASE; PROTEIN RESD; PROTEIN RESE; UNCLASSIFIED DRUG;

EID: 1542376961     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.6.1694-1704.2004     Document Type: Article
Times cited : (20)

References (43)
  • 1
    • 0037216619 scopus 로고    scopus 로고
    • Mutational analysis of a conserved signal-transducing element: The HAMP linker of the Escherichia coli nitrate sensor NarX
    • Appleman, J. A., and V. Stewart. 2003. Mutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarX. J. Bacteriol. 185:89-97.
    • (2003) J. Bacteriol. , vol.185 , pp. 89-97
    • Appleman, J.A.1    Stewart, V.2
  • 2
    • 0025151973 scopus 로고
    • Sugars induce the Agrobacterium virulence genes through a periplasmic binding protein and a transmembrane signal protein
    • Cangelosi, G. A., R. C. Ankenbauer, and E. W. Nester. 1990. Sugars induce the Agrobacterium virulence genes through a periplasmic binding protein and a transmembrane signal protein. Proc. Natl. Acad. Sci. USA 87:6708-6712.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6708-6712
    • Cangelosi, G.A.1    Ankenbauer, R.C.2    Nester, E.W.3
  • 3
    • 0029843812 scopus 로고    scopus 로고
    • Role of the periplasmic domain of the Escherichia coli NarX sensor-transmitter protein in nitrate-dependent signal transduction and gene regulation
    • Cavicchioli, R., R. C. Chiang, L. V. Kalman, and R. P. Gunsalus. 1996. Role of the periplasmic domain of the Escherichia coli NarX sensor-transmitter protein in nitrate-dependent signal transduction and gene regulation. Mol. Microbiol. 21:901-911.
    • (1996) Mol. Microbiol. , vol.21 , pp. 901-911
    • Cavicchioli, R.1    Chiang, R.C.2    Kalman, L.V.3    Gunsalus, R.P.4
  • 5
    • 0026698151 scopus 로고
    • Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein
    • Chang, C.-H., and S. C. Winans. 1992. Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein. J. Bacteriol. 174:7033-7039.
    • (1992) J. Bacteriol. , vol.174 , pp. 7033-7039
    • Chang, C.-H.1    Winans, S.C.2
  • 6
    • 0026740927 scopus 로고
    • Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli
    • Chiang, R. C., R. Cavicchioli, and R. P. Gunsalus. 1992. Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli. Mol. Microbiol. 6:1913-1923.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1913-1923
    • Chiang, R.C.1    Cavicchioli, R.2    Gunsalus, R.P.3
  • 7
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal transduction in Bacillus subtilis: How one organism sees its world
    • Fabret, C., V. A. Feher, and J. A. Hoch. 1999. Two-component signal transduction in Bacillus subtilis: how one organism sees its world. J. Bacteriol. 181:1975-1983.
    • (1999) J. Bacteriol. , vol.181 , pp. 1975-1983
    • Fabret, C.1    Feher, V.A.2    Hoch, J.A.3
  • 8
    • 0035933597 scopus 로고    scopus 로고
    • Quinones as the redox signal for the arc two-component system of bacteria
    • Georgellis, D., O. Kwon, and E. C. C. Lin. 2001. Quinones as the redox signal for the arc two-component system of bacteria. Science 292:2314-2316.
    • (2001) Science , vol.292 , pp. 2314-2316
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.C.3
  • 9
    • 0035212488 scopus 로고    scopus 로고
    • Redox signal transduction by the ArcB sensor kinase of Haemophilus influenzae lacking the PAS domain
    • Georgellis, D., O. Kwon, E. C. C. Lin, S. M. Wong, and B. J. Akerley. 2001. Redox signal transduction by the ArcB sensor kinase of Haemophilus influenzae lacking the PAS domain. J. Bacteriol. 183:7206-7212.
    • (2001) J. Bacteriol. , vol.183 , pp. 7206-7212
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.C.3    Wong, S.M.4    Akerley, B.J.5
  • 11
    • 0032781275 scopus 로고    scopus 로고
    • The periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
    • Kaspar, S., R. Perozzo, S. Reinelt, M. Meyer, K. Pfister, L. Scapozza, and M. Bott. 1999. The periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor. Mol. Microbiol. 33:858-872.
    • (1999) Mol. Microbiol. , vol.33 , pp. 858-872
    • Kaspar, S.1    Perozzo, R.2    Reinelt, S.3    Meyer, M.4    Pfister, K.5    Scapozza, L.6    Bott, M.7
  • 12
    • 0032835113 scopus 로고    scopus 로고
    • Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: Nitrate elicits a superior anion ligand response compared to nitrite
    • Lee, A. I., A. Delgado, and R. P. Gunsalus. 1999. Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: nitrate elicits a superior anion ligand response compared to nitrite. J. Bacteriol. 181:5309-5316.
    • (1999) J. Bacteriol. , vol.181 , pp. 5309-5316
    • Lee, A.I.1    Delgado, A.2    Gunsalus, R.P.3
  • 13
  • 14
    • 0026511245 scopus 로고
    • The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain
    • Monson, E. K., M. Weinstein, G. S. Ditta, and D. R. Helinski. 1992. The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain. Proc. Natl. Acad. Sci. USA 89:4280-4284.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4280-4284
    • Monson, E.K.1    Weinstein, M.2    Ditta, G.S.3    Helinski, D.R.4
  • 15
    • 0036189830 scopus 로고    scopus 로고
    • Induction of ResDE-dependent gene expression in Bacillus subtilis in response to nitric oxide and nitrosative stress
    • Nakano, M. M. 2002. Induction of ResDE-dependent gene expression in Bacillus subtilis in response to nitric oxide and nitrosative stress. J. Bacteriol. 184:1783-1787.
    • (2002) J. Bacteriol. , vol.184 , pp. 1783-1787
    • Nakano, M.M.1
  • 16
    • 0030700663 scopus 로고    scopus 로고
    • Characterization of anaerobic fermentative growth in Bacillus subtilis: Identification of fermentation end products and genes required for the growth
    • Nakano, M. M., Y. P. Dailly, P. Zuber, and D. P. Clark. 1997. Characterization of anaerobic fermentative growth in Bacillus subtilis: identification of fermentation end products and genes required for the growth. J. Bacteriol. 179:6749-6755.
    • (1997) J. Bacteriol. , vol.179 , pp. 6749-6755
    • Nakano, M.M.1    Dailly, Y.P.2    Zuber, P.3    Clark, D.P.4
  • 17
    • 0024243827 scopus 로고
    • Identification of a genetic locus required for biosynthesis of the lipopeptide antibiotic surfactin in Bacillus subtilis
    • Nakano, M. M., M. A. Marahiel, and P. Zuber. 1988. Identification of a genetic locus required for biosynthesis of the lipopeptide antibiotic surfactin in Bacillus subtilis. J. Bacteriol. 170:5662-5668.
    • (1988) J. Bacteriol. , vol.170 , pp. 5662-5668
    • Nakano, M.M.1    Marahiel, M.A.2    Zuber, P.3
  • 18
    • 0028932022 scopus 로고
    • Nitrogen regulation of nasA and the nasB operon, which encode genes required for nitrate assimilation in Bacillus subtilis
    • Nakano, M. M., F. Yang, P. Hardin, and P. Zuber. 1995. Nitrogen regulation of nasA and the nasB operon, which encode genes required for nitrate assimilation in Bacillus subtilis. J. Bacteriol. 177:573-579.
    • (1995) J. Bacteriol. , vol.177 , pp. 573-579
    • Nakano, M.M.1    Yang, F.2    Hardin, P.3    Zuber, P.4
  • 19
    • 0035104390 scopus 로고    scopus 로고
    • Involvement of the ResE phosphatase activity in down-regulation of ResD-controlled genes in Bacillus subtilis during aerobic growth
    • Nakano, M. M., and Y. Zhu. 2001. Involvement of the ResE phosphatase activity in down-regulation of ResD-controlled genes in Bacillus subtilis during aerobic growth. J. Bacteriol. 183:1938-1944.
    • (2001) J. Bacteriol. , vol.183 , pp. 1938-1944
    • Nakano, M.M.1    Zhu, Y.2
  • 20
    • 0033812771 scopus 로고    scopus 로고
    • Interaction of ResD with regulatory regions of anaerobically induced genes in Bacillus subtilis
    • Nakano, M. M., Y. Zhu, M. LaCelle, X. Zhang, and F. M. Hulett. 2000. Interaction of ResD with regulatory regions of anaerobically induced genes in Bacillus subtilis. Mol. Microbiol. 37:1198-1207.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1198-1207
    • Nakano, M.M.1    Zhu, Y.2    LaCelle, M.3    Zhang, X.4    Hulett, F.M.5
  • 21
    • 0031727390 scopus 로고    scopus 로고
    • Anaerobic growth of a "strict aerobe" (Bacillus subtilis)
    • Nakano, M. M., and P. Zuber. 1998. Anaerobic growth of a "strict aerobe" (Bacillus subtilis). Annu. Rev. Microbiol. 52:165-190.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 165-190
    • Nakano, M.M.1    Zuber, P.2
  • 22
    • 0029889199 scopus 로고    scopus 로고
    • Two-component regulatory proteins ResD-ResE are required for transcriptional activation of fnr upon oxygen limitation in Bacillus subtilis
    • Nakano, M. M., P. Zuber, P. Glaser, A. Danchin, and F. M. Hulett. 1996. Two-component regulatory proteins ResD-ResE are required for transcriptional activation of fnr upon oxygen limitation in Bacillus subtilis. J. Bacteriol. 178:3796-3802.
    • (1996) J. Bacteriol. , vol.178 , pp. 3796-3802
    • Nakano, M.M.1    Zuber, P.2    Glaser, P.3    Danchin, A.4    Hulett, F.M.5
  • 23
    • 0035164698 scopus 로고    scopus 로고
    • The default state of the membrane-localized histidine kinase PrrB of Rhodobacter sphaeroides 2.4.1 is in the kinase-positive mode
    • Oh, J. I., I. J. Ko, and S. Kaplan. 2001. The default state of the membrane-localized histidine kinase PrrB of Rhodobacter sphaeroides 2.4.1 is in the kinase-positive mode. J. Bacteriol. 183:6807-6814.
    • (2001) J. Bacteriol. , vol.183 , pp. 6807-6814
    • Oh, J.I.1    Ko, I.J.2    Kaplan, S.3
  • 24
    • 0030811371 scopus 로고    scopus 로고
    • Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli
    • Park, H., and M. Inouye. 1997. Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli. J. Bacteriol. 179:4382-4390.
    • (1997) J. Bacteriol. , vol.179 , pp. 4382-4390
    • Park, H.1    Inouye, M.2
  • 25
    • 0032791524 scopus 로고    scopus 로고
    • Mutational analysis and membrane topology of ComP, a quorum-sensing histidine kinase of Bacillus subtilis controlling competence development
    • Piazza, F., P. Tortosa, and D. Dubnau. 1999. Mutational analysis and membrane topology of ComP, a quorum-sensing histidine kinase of Bacillus subtilis controlling competence development. J. Bacteriol. 181:4540-4548.
    • (1999) J. Bacteriol. , vol.181 , pp. 4540-4548
    • Piazza, F.1    Tortosa, P.2    Dubnau, D.3
  • 26
    • 0036296323 scopus 로고    scopus 로고
    • Expression, purification and characterisation of full-length histidine protein kinase RegB from Rhodobacter sphaeroides
    • Potter, C. A., A. Ward, C. Laguri, M. P. Williamson, P. J. Henderson, and M. K. Phillips-Jones. 2002. Expression, purification and characterisation of full-length histidine protein kinase RegB from Rhodobacter sphaeroides. J. Mol. Biol. 320:201-213.
    • (2002) J. Mol. Biol. , vol.320 , pp. 201-213
    • Potter, C.A.1    Ward, A.2    Laguri, C.3    Williamson, M.P.4    Henderson, P.J.5    Phillips-Jones, M.K.6
  • 27
    • 0141643091 scopus 로고    scopus 로고
    • The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain
    • Reinelt, S., E. Hofmann, T. Gerharz, M. Bott, and D. R. Madden. 2003. The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain. J. Biol. Chem. 278:39189-39196.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39189-39196
    • Reinelt, S.1    Hofmann, E.2    Gerharz, T.3    Bott, M.4    Madden, D.R.5
  • 28
    • 0032920056 scopus 로고    scopus 로고
    • The cytoplasmic kinase domain of PhoR is sufficient for the low phosphate-inducible expression of pho regulon genes in Bacillus subtilis
    • Shi, L., and F. M. Hulett. 1999. The cytoplasmic kinase domain of PhoR is sufficient for the low phosphate-inducible expression of pho regulon genes in Bacillus subtilis. Mol. Microbiol. 31:211-222.
    • (1999) Mol. Microbiol. , vol.31 , pp. 211-222
    • Shi, L.1    Hulett, F.M.2
  • 30
    • 0032752641 scopus 로고    scopus 로고
    • Negatively charged phospholipids influence the activity of the sensor kinase KdpD of Escherichia coli
    • Stallkamp, I., W. Dowhan, K. Altendorf, and K. Jung. 1999. Negatively charged phospholipids influence the activity of the sensor kinase KdpD of Escherichia coli. Arch. Microbiol. 172:295-302.
    • (1999) Arch. Microbiol. , vol.172 , pp. 295-302
    • Stallkamp, I.1    Dowhan, W.2    Altendorf, K.3    Jung, K.4
  • 31
    • 0035910008 scopus 로고    scopus 로고
    • PAS-A domain of phosphorelay sensor kinase A: A catalytic ATP-binding domain involved in the initiation of development in Bacillus subtilis
    • Stephenson, K., and J. A. Hoch. 2001. PAS-A domain of phosphorelay sensor kinase A: a catalytic ATP-binding domain involved in the initiation of development in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 98:15251-15256.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15251-15256
    • Stephenson, K.1    Hoch, J.A.2
  • 32
    • 0023853759 scopus 로고
    • Processing of a sporulation factor in Bacillus subtilis: How morphological structure could control gene expression
    • Stragier, P., C. Bonamy, and C. Karmazyn-Campelli. 1988. Processing of a sporulation factor in Bacillus subtilis: how morphological structure could control gene expression. Cell 52:697-704.
    • (1988) Cell , vol.52 , pp. 697-704
    • Stragier, P.1    Bonamy, C.2    Karmazyn-Campelli, C.3
  • 35
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L., and I. B. Zhulin. 1999. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 37
    • 0029967951 scopus 로고    scopus 로고
    • Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants
    • Waldburger, C. D., and R. T. Sauer. 1996. Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants. J. Biol. Chem. 271:26630-26636.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26630-26636
    • Waldburger, C.D.1    Sauer, R.T.2
  • 38
    • 0027532540 scopus 로고
    • Phosphorylation and dephosphorylation catalyzed in vitro by purified components of the nitrate sensing system, NarX and NarL
    • Walker, M., and J. A. DeMoss. 1993. Phosphorylation and dephosphorylation catalyzed in vitro by purified components of the nitrate sensing system, NarX and NarL. J. Biol. Chem. 268:8391-8393.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8391-8393
    • Walker, M.1    DeMoss, J.A.2
  • 39
    • 0035045569 scopus 로고    scopus 로고
    • Dissection of the functional and structural domains of phosphorelay histidine kinase A of Bacillus subtilis
    • Wang, L., C. Fabret, K. Kanamaru, K. Stephenson, V. Dartois, M. Perego, and J. A. Hoch. 2001. Dissection of the functional and structural domains of phosphorelay histidine kinase A of Bacillus subtilis. J. Bacteriol. 183:2795-2802.
    • (2001) J. Bacteriol. , vol.183 , pp. 2795-2802
    • Wang, L.1    Fabret, C.2    Kanamaru, K.3    Stephenson, K.4    Dartois, V.5    Perego, M.6    Hoch, J.A.7
  • 40
    • 0032880016 scopus 로고    scopus 로고
    • Identification of a conserved N-terminal sequence involved in transmembrane signal transduction in EnvZ
    • Waukau, J., and S. Forst. 1999. Identification of a conserved N-terminal sequence involved in transmembrane signal transduction in EnvZ. J. Bacteriol. 181:5534-5538.
    • (1999) J. Bacteriol. , vol.181 , pp. 5534-5538
    • Waukau, J.1    Forst, S.2
  • 41
    • 0032826834 scopus 로고    scopus 로고
    • Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction
    • Williams, S. B., and V. Stewart. 1999. Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction. Mol. Microbiol. 33:1093-1102.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1093-1102
    • Williams, S.B.1    Stewart, V.2
  • 42
    • 0033759718 scopus 로고    scopus 로고
    • The histidine kinase domain of UhpB inhibits UhpA action at the Escherichia coli uhpT promoter
    • Wright, J. S., I. N. Olekhnovich, G. Touchie, and R. J. Kadner. 2000. The histidine kinase domain of UhpB inhibits UhpA action at the Escherichia coli uhpT promoter. J. Bacteriol. 182:6279-6286.
    • (2000) J. Bacteriol. , vol.182 , pp. 6279-6286
    • Wright, J.S.1    Olekhnovich, I.N.2    Touchie, G.3    Kadner, R.J.4
  • 43
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox
    • Zhulin, I. B., B. L. Taylor, and R. Dixon. 1997. PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 22:331-333.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.