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Journal of Bacteriology
Volumn 196, Issue 9, 2014, Pages 1741-1752
The PhoU protein from Escherichia coli interacts with PhoR, PstB, and metals to form a phosphate-signaling complex at the membrane
Author keywords

[No Author keywords available]
Indexed keywords

BACTERIAL PROTEIN; MAGNESIUM; MANGANESE; METAL; PHOR PROTEIN; PHOSPHATE; PHOU PROTEIN; PSTB PROTEIN; UNCLASSIFIED DRUG;
EID: 84897505593     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00029-14     Document Type: Article
Times cited : (78)
References (67)
  • 1
    • 77949915670 scopus 로고    scopus 로고
    • Global regulation by the seven-component Pi signaling system
    • Hsieh YJ, Wanner BL. 2010. Global regulation by the seven-component Pi signaling system. Curr. Opin. Microbiol. 13:198-203. http://dx.doi.org/10.1016/j.mib.2010.01.014.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 198-203
    • Hsieh, Y.J.1    Wanner, B.L.2
  • 2
    • 0003338719 scopus 로고    scopus 로고
    • Phosphorous assimilation and control of the phosphate regulon
    • Neidhardt FC, Curtiss R, III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed), 2nd ed. ASM Press, Washington, DC.
    • Wanner BL. 1996. Phosphorous assimilation and control of the phosphate regulon, p 1357-1381. In Neidhardt FC, Curtiss R, III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, UmbargerHE(ed), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: cellular and molecular biology , pp. 1357-1381
    • Wanner, B.L.1
  • 3
    • 0025079661 scopus 로고
    • Molecular aspects of phosphate transport in Escherichia coli
    • Rao NN, Torriani A. 1990. Molecular aspects of phosphate transport in Escherichia coli. Mol. Microbiol. 4:1083-1090. http://dx.doi.org/10.1111/j.1365-2958.1990.tb00682.x.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1083-1090
    • Rao, N.N.1    Torriani, A.2
  • 4
    • 0342269112 scopus 로고
    • The birth of the Pho regulon
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A, Yagil E (ed). American Society for Microbiology, Washington, DC.
    • Torriani-Gorini A. 1987. The birth of the Pho regulon, p 3-11. In Torriani-Gorini A, Rothman FG, Silver S, Wright A, Yagil E (ed), Phosphate metabolism and cellular regulation in microorganisms. American Society for Microbiology, Washington, DC.
    • (1987) Phosphate metabolism and cellular regulation in microorganisms , pp. 3-11
    • Torriani-Gorini, A.1
  • 5
    • 0027411096 scopus 로고
    • Gene regulation by phosphate in enteric bacteria
    • Wanner BL. 1993. Gene regulation by phosphate in enteric bacteria. J. Cell. Biochem. 51:47-54. http://dx.doi.org/10.1002/jcb.240510110.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 47-54
    • Wanner, B.L.1
  • 6
    • 0024811077 scopus 로고
    • Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins
    • Makino K, Shinagawa H, Amemura M, Kawamoto T, Yamada M, Nakata A. 1989. Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins. J. Mol. Biol. 210:551-559. http://dx.doi.org/10.1016/0022-2836(89)90131-9.
    • (1989) J. Mol. Biol. , vol.210 , pp. 551-559
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Kawamoto, T.4    Yamada, M.5    Nakata, A.6
  • 7
    • 24344476732 scopus 로고    scopus 로고
    • Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states
    • Bachhawat P, Swapna GV, Montelione GT, Stock AM. 2005. Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states. Structure (Camb.) 13:1353-1363. http://dx.doi.org/10.1016/j.str.2005.06.006.
    • (2005) Structure (Camb.) , vol.13 , pp. 1353-1363
    • Bachhawat, P.1    Swapna, G.V.2    Montelione, G.T.3    Stock, A.M.4
  • 8
    • 0027339446 scopus 로고
    • Role of the σ70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli
    • Makino K, Amemura M, Kim S, Nakata A, Shinagawa H. 1993. Role of the σ70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli. Genes Dev. 7:149-160. http://dx.doi.org/10.1101/gad.7.1.149.
    • (1993) Genes Dev. , vol.7 , pp. 149-160
    • Makino, K.1    Amemura, M.2    Kim, S.3    Nakata, A.4    Shinagawa, H.5
  • 9
    • 0022533109 scopus 로고
    • Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12
    • Makino K, Shinagawa H, Amemura M, Nakata A. 1986. Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12. J. Mol. Biol. 190:37-44. http://dx.doi.org/10.1016/0022-2836(86)90073-2.
    • (1986) J. Mol. Biol. , vol.190 , pp. 37-44
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Nakata, A.4
  • 10
    • 0029896773 scopus 로고    scopus 로고
    • The activation of Pho B byacetylphosphate
    • McClearyWR.1996.Theactivation ofPhoBbyacetylphosphate.Mol.Microbiol. 20:1155-1163. http://dx.doi.org/10.1111/j.1365-2958.1996.tb02636.x.
    • (1996) Mol.Microbiol. , vol.20 , pp. 1155-1163
    • McCleary, W.R.1
  • 11
    • 0037309136 scopus 로고    scopus 로고
    • Genetic and biochemical studies of phosphatase activity of PhoR
    • Carmany DO, Hollingsworth K, McCleary WR. 2003. Genetic and biochemical studies of phosphatase activity of PhoR. J. Bacteriol. 185:1112-1115. http://dx.doi.org/10.1128/JB.185.3.1112-1115.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 1112-1115
    • Carmany, D.O.1    Hollingsworth, K.2    McCleary, W.R.3
  • 12
    • 0022977821 scopus 로고
    • Nucleotide sequence of the phoR gene, a regulatory gene for the phosphate regulon of Escherichia coli
    • Makino K, Shinagawa H, Amemura M, Nakata A. 1986. Nucleotide sequence of the phoR gene, a regulatory gene for the phosphate regulon of Escherichia coli. J. Mol. Biol. 192:549-556. http://dx.doi.org/10.1016/0022-2836(86)90275-5.
    • (1986) J. Mol. Biol. , vol.192 , pp. 549-556
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Nakata, A.4
  • 14
    • 0032730205 scopus 로고    scopus 로고
    • Histidine kinases: diversity of domain organization
    • Dutta R, Qin L, Inouye M. 1999. Histidine kinases: diversity of domain organization. Mol. Microbiol. 34:633-640. http://dx.doi.org/10.1046/j.1365-2958.1999.01646.x.
    • (1999) Mol. Microbiol. , vol.34 , pp. 633-640
    • Dutta, R.1    Qin, L.2    Inouye, M.3
  • 15
    • 0027507211 scopus 로고
    • Effect of glpT and glpD mutations on expression of the phoA gene in Escherichia coli
    • Rao NN, Roberts MF, Torriani A, Yashphe J. 1993. Effect of glpT and glpD mutations on expression of the phoA gene in Escherichia coli. J. Bacteriol. 175:74-79.
    • (1993) J. Bacteriol. , vol.175 , pp. 74-79
    • Rao, N.N.1    Roberts, M.F.2    Torriani, A.3    Yashphe, J.4
  • 17
    • 27744450676 scopus 로고    scopus 로고
    • Escherichia coli starvation diets: essential nutrients weigh in distinctly
    • Peterson CN, Mandel MJ, Silhavy TJ. 2005. Escherichia coli starvation diets: essential nutrients weigh in distinctly. J. Bacteriol. 187:7549-7553. http://dx.doi.org/10.1128/JB.187.22.7549-7553.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 7549-7553
    • Peterson, C.N.1    Mandel, M.J.2    Silhavy, T.J.3
  • 18
    • 0021881068 scopus 로고
    • Nucleotide sequence of the genes involved in phosphate transport and regulation of the phosphate regulon in E. coli
    • Amemura M, Makino K, Shinagawa H, Kobayashi A, Nakata A. 1985. Nucleotide sequence of the genes involved in phosphate transport and regulation of the phosphate regulon in E. coli. J. Mol. Biol. 184:241-250. http://dx.doi.org/10.1016/0022-2836(85)90377-8.
    • (1985) J. Mol. Biol. , vol.184 , pp. 241-250
    • Amemura, M.1    Makino, K.2    Shinagawa, H.3    Kobayashi, A.4    Nakata, A.5
  • 19
  • 20
    • 0026491079 scopus 로고
    • Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters
    • Webb DC, Rosenberg H, Cox GB. 1992. Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters. J. Biol. Chem. 267:24661-24668.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24661-24668
    • Webb, D.C.1    Rosenberg, H.2    Cox, G.B.3
  • 21
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson AL, Dassa E, Orelle C, Chen J. 2008. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72:317-364. http://dx.doi.org/10.1128/MMBR.00031-07.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 22
    • 0027441190 scopus 로고
    • Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU protein in the phosphate regulon
    • Steed PM, Wanner BL. 1993. Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU protein in the phosphate regulon. J. Bacteriol. 175:6797-6809.
    • (1993) J. Bacteriol. , vol.175 , pp. 6797-6809
    • Steed, P.M.1    Wanner, B.L.2
  • 23
    • 59649094128 scopus 로고    scopus 로고
    • Employment of a promoter-swapping technique shows that PhoU modulates the activity of the PstSCAB2 ABC transporter in Escherichia coli
    • Rice CD, Pollard JE, Lewis ZT, McCleary WR. 2009. Employment of a promoter-swapping technique shows that PhoU modulates the activity of the PstSCAB2 ABC transporter in Escherichia coli. Appl. Environ. Microbiol. 75:573-582. http://dx.doi.org/10.1128/AEM.01046-08.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 573-582
    • Rice, C.D.1    Pollard, J.E.2    Lewis, Z.T.3    McCleary, W.R.4
  • 24
    • 0023027010 scopus 로고
    • Purification of the PhoU protein, a negative regulator of the pho regulon of Escherichia coli K-12
    • Surin BP, Dixon NE, Rosenberg H. 1986. Purification of the PhoU protein, a negative regulator of the pho regulon of Escherichia coli K-12. J. Bacteriol. 168:631-635.
    • (1986) J. Bacteriol. , vol.168 , pp. 631-635
    • Surin, B.P.1    Dixon, N.E.2    Rosenberg, H.3
  • 25
    • 18144379106 scopus 로고    scopus 로고
    • Crystal structure of a PhoU protein homologue: a new class of metalloprotein containing multinuclear iron clusters
    • Liu J, Lou Y, Yokota H, Adams PD, Kim R, Kim SH. 2005. Crystal structure of a PhoU protein homologue: a new class of metalloprotein containing multinuclear iron clusters. J. Biol. Chem. 280:15960-15966. http://dx.doi.org/10.1074/jbc.M414117200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15960-15966
    • Liu, J.1    Lou, Y.2    Yokota, H.3    Adams, P.D.4    Kim, R.5    Kim, S.H.6
  • 27
    • 20444450864 scopus 로고    scopus 로고
    • Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus
    • Oganesyan V, Oganesyan N, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH. 2005. Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus. J. Bacteriol. 187:4238-4244. http://dx.doi.org/10.1128/JB.187.12.4238-4244.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 4238-4244
    • Oganesyan, V.1    Oganesyan, N.2    Adams, P.D.3    Jancarik, J.4    Yokota, H.A.5    Kim, R.6    Kim, S.H.7
  • 28
    • 0034811824 scopus 로고    scopus 로고
    • The phosphate-binding protein of Escherichia coli is not essential for Pi-regulated expression of the pho regulon
    • Hoffer SM, Tommassen J. 2001. The phosphate-binding protein of Escherichia coli is not essential for Pi-regulated expression of the pho regulon. J. Bacteriol. 183:5768-5771. http://dx.doi.org/10.1128/JB.183.19.5768-5771.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 5768-5771
    • Hoffer, S.M.1    Tommassen, J.2
  • 29
    • 0022454125 scopus 로고
    • Nucleotide pool in pho regulon mutants and alkaline phosphatase synthesis in E. coli
    • Rao NN, Wang E, Yashphe J, Torriani A. 1986. Nucleotide pool in pho regulon mutants and alkaline phosphatase synthesis in E. coli. J. Bacteriol. 166:205-211.
    • (1986) J. Bacteriol. , vol.166 , pp. 205-211
    • Rao, N.N.1    Wang, E.2    Yashphe, J.3    Torriani, A.4
  • 30
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645. http://dx.doi.org/10.1073/pnas.120163297.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 32
    • 0024453564 scopus 로고
    • Regulation of the phosphate regulon of Escherichia coli: analysis of mutant phoB and phoR genes causing different phenotypes
    • Yamada M, Makino K, Amemura M, Shinagawa H, Nakata A. 1989. Regulation of the phosphate regulon of Escherichia coli: analysis of mutant phoB and phoR genes causing different phenotypes. J. Bacteriol. 171:5601-5606.
    • (1989) J. Bacteriol. , vol.171 , pp. 5601-5606
    • Yamada, M.1    Makino, K.2    Amemura, M.3    Shinagawa, H.4    Nakata, A.5
  • 33
    • 33646597727 scopus 로고    scopus 로고
    • Loss-and gain-offunction mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer
    • Buron-Barral MC, Gosink KK, Parkinson JS. 2006. Loss-and gain-offunction mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer. J. Bacteriol. 188:3477-3486. http://dx.doi.org/10.1128/JB.188.10.3477-3486.2006.
    • (2006) J. Bacteriol. , vol.188 , pp. 3477-3486
    • Buron-Barral, M.C.1    Gosink, K.K.2    Parkinson, J.S.3
  • 34
    • 27344455900 scopus 로고    scopus 로고
    • Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies
    • Studdert CA, Parkinson JS. 2005. Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies. Proc. Natl. Acad. Sci. U. S. A. 102:15623-15628. http://dx.doi.org/10.1073/pnas.0506040102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15623-15628
    • Studdert, C.A.1    Parkinson, J.S.2
  • 35
    • 0025873742 scopus 로고
    • Allelic exchange in Escherichia coli using the Bacillus subtilis sacB gene and a temperaturesensitive pSC101 replicon
    • Blomfield IC, Vaughn V, Rest RF, Eisenstein BI. 1991. Allelic exchange in Escherichia coli using the Bacillus subtilis sacB gene and a temperaturesensitive pSC101 replicon. Mol. Microbiol. 5:1447-1457. http://dx.doi.org/10.1111/j.1365-2958.1991.tb00791.x.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1447-1457
    • Blomfield, I.C.1    Vaughn, V.2    Rest, R.F.3    Eisenstein, B.I.4
  • 38
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4:363-371. http://dx.doi.org/10.1038/nprot.2009.2.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 39
    • 84872386731 scopus 로고    scopus 로고
    • The bacterial two-hybrid system based on adenylate cyclase reconstitution in Escherichia coli
    • Battesti A, Bouveret E. 2012. The bacterial two-hybrid system based on adenylate cyclase reconstitution in Escherichia coli. Methods 58:325-334. http://dx.doi.org/10.1016/j.ymeth.2012.07.018.
    • (2012) Methods , vol.58 , pp. 325-334
    • Battesti, A.1    Bouveret, E.2
  • 40
    • 0036291504 scopus 로고    scopus 로고
    • Measuring beta-galactosidase activity in bacteria: cell growth, permeabilization, and enzyme assays in 96-well arrays
    • Griffith KL, Wolf RE, Jr. 2002. Measuring beta-galactosidase activity in bacteria: cell growth, permeabilization, and enzyme assays in 96-well arrays. Biochem. Biophys. Res. Commun. 290:397-402. http://dx.doi.org/10.1006/bbrc.2001.6152.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 397-402
    • Griffith, K.L.1    Wolf Jr., R.E.2
  • 41
    • 1542346163 scopus 로고    scopus 로고
    • High-throughput betagalactosidase assay for bacterial cell-based reporter systems
    • Thibodeau SA, Fang R, Joung JK. 2004. High-throughput betagalactosidase assay for bacterial cell-based reporter systems. Biotechniques 36:410-415.
    • (2004) Biotechniques , vol.36 , pp. 410-415
    • Thibodeau, S.A.1    Fang, R.2    Joung, J.K.3
  • 42
    • 0032428036 scopus 로고    scopus 로고
    • Analysis of the conserved acidic residues in the regulatory domain of PhoB
    • Zundel CJ, Capener DC, McCleary WR. 1998. Analysis of the conserved acidic residues in the regulatory domain of PhoB. FEBS Lett. 441:242-246. http://dx.doi.org/10.1016/S0014-5793(98)01556-7.
    • (1998) FEBS Lett. , vol.441 , pp. 242-246
    • Zundel, C.J.1    Capener, D.C.2    McCleary, W.R.3
  • 43
    • 0141995016 scopus 로고    scopus 로고
    • Constitutive activation of the Escherichia coli Pho regulon upregulates rpoS translation in an Hfq-dependent fashion
    • Ruiz N, Silhavy TJ. 2003. Constitutive activation of the Escherichia coli Pho regulon upregulates rpoS translation in an Hfq-dependent fashion. J. Bacteriol. 185:5984-5992. http://dx.doi.org/10.1128/JB.185.20.5984-5992.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 5984-5992
    • Ruiz, N.1    Silhavy, T.J.2
  • 44
    • 33846617433 scopus 로고    scopus 로고
    • Genetic evidence suggests that the intergenic region between pstA and pstB plays a role in the regulation of rpoS translation during phosphate limitation
    • Schurdell MS, Woodbury GM, McCleary WR. 2007. Genetic evidence suggests that the intergenic region between pstA and pstB plays a role in the regulation of rpoS translation during phosphate limitation. J. Bacteriol. 189:1150-1153. http://dx.doi.org/10.1128/JB.01482-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 1150-1153
    • Schurdell, M.S.1    Woodbury, G.M.2    McCleary, W.R.3
  • 46
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian JT, Callis PR. 2001. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80:2093-2109. http://dx.doi.org/10.1016/S0006-3495(01)76183-8.
    • (2001) Biophys. J. , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 47
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem A, Varghese S, Imlay JA. 2009. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 72:844-858. http://dx.doi.org/10.1111/j.1365-2958.2009.06699.x.
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 48
    • 80055048346 scopus 로고    scopus 로고
    • The Escherichia coli MntR miniregulon includes genes encoding a small protein and an efflux pump required for manganese homeostasis
    • Waters LS, Sandoval M, Storz G. 2011. The Escherichia coli MntR miniregulon includes genes encoding a small protein and an efflux pump required for manganese homeostasis. J. Bacteriol. 193:5887-5897. http://dx.doi.org/10.1128/JB.05872-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 5887-5897
    • Waters, L.S.1    Sandoval, M.2    Storz, G.3
  • 49
    • 33845916036 scopus 로고    scopus 로고
    • Metal binding studies and EPR spectroscopy of the manganese transport regulator MntR
    • Golynskiy MV, Gunderson WA, Hendrich MP, Cohen SM. 2006. Metal binding studies and EPR spectroscopy of the manganese transport regulator MntR. Biochemistry 45:15359-15372. http://dx.doi.org/10.1021/bi0607406.
    • (2006) Biochemistry , vol.45 , pp. 15359-15372
    • Golynskiy, M.V.1    Gunderson, W.A.2    Hendrich, M.P.3    Cohen, S.M.4
  • 50
    • 0001388699 scopus 로고
    • Manganese active transport in Escherichia coli
    • Silver S, Johnseine P, King K. 1970. Manganese active transport in Escherichia coli. J. Bacteriol. 104:1299-1306.
    • (1970) J. Bacteriol. , vol.104 , pp. 1299-1306
    • Silver, S.1    Johnseine, P.2    King, K.3
  • 51
    • 0021929046 scopus 로고
    • Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187
    • Alatossava T, Jutte H, Kuhn A, Kellenberger E. 1985. Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187. J. Bacteriol. 162:413-419.
    • (1985) J. Bacteriol. , vol.162 , pp. 413-419
    • Alatossava, T.1    Jutte, H.2    Kuhn, A.3    Kellenberger, E.4
  • 52
    • 12144288910 scopus 로고    scopus 로고
    • Cysteine mediated multimerization of a recombinant dengue E fragment fused to the P64k protein following immobilized metal ion affinity chromatography
    • Lopez C, Sanchez J, Hermida L, Zulueta A, Marquez G. 2004. Cysteine mediated multimerization of a recombinant dengue E fragment fused to the P64k protein following immobilized metal ion affinity chromatography. Protein Expr. Purif. 34:176-182. http://dx.doi.org/10.1016/j.pep.2003.11.018.
    • (2004) Protein Expr. Purif. , vol.34 , pp. 176-182
    • Lopez, C.1    Sanchez, J.2    Hermida, L.3    Zulueta, A.4    Marquez, G.5
  • 53
    • 70349777587 scopus 로고    scopus 로고
    • Structure and signaling mechanism of Per-ARNT-Sim domains
    • Moglich A, Ayers RA, Moffat K. 2009. Structure and signaling mechanism of Per-ARNT-Sim domains. Structure 17:1282-1294. http://dx.doi.org/10.1016/j.str.2009.08.011.
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Moglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 54
    • 84872817053 scopus 로고    scopus 로고
    • Signal transduction and phosphoryl transfer by a FixL hybrid kinase with low oxygen affinity: importance of the vicinal PAS domain and receiver aspartate
    • Sousa EH, Tuckerman JR, Gondim AC, Gonzalez G, Gilles-Gonzalez MA. 2013. Signal transduction and phosphoryl transfer by a FixL hybrid kinase with low oxygen affinity: importance of the vicinal PAS domain and receiver aspartate. Biochemistry 52:456-565. http://dx.doi.org/10.1021/bi300991r.
    • (2013) Biochemistry , vol.52 , pp. 456-565
    • Sousa, E.H.1    Tuckerman, J.R.2    Gondim, A.C.3    Gonzalez, G.4    Gilles-Gonzalez, M.A.5
  • 56
    • 84878093352 scopus 로고    scopus 로고
    • Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA
    • Winnen B, Anderson E, Cole JL, King GF, Rowland SL. 2013. Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA. J. Bacteriol. 195:2349-2358. http://dx.doi.org/10.1128/JB.00096-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 2349-2358
    • Winnen, B.1    Anderson, E.2    Cole, J.L.3    King, G.F.4    Rowland, S.L.5
  • 57
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of twocomponent proteins
    • Gao R, Stock AM. 2009. Biological insights from structures of twocomponent proteins. Annu. Rev. Microbiol. 63:133-154. http://dx.doi.org/10.1146/annurev.micro.091208.073214.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 58
    • 36549003158 scopus 로고    scopus 로고
    • Sensor complexes regulating two-component signal transduction
    • Szurmant H, White RA, Hoch JA. 2007. Sensor complexes regulating two-component signal transduction. Curr. Opin. Struct. Biol. 17:706-715. http://dx.doi.org/10.1016/j.sbi.2007.08.019.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 706-715
    • Szurmant, H.1    White, R.A.2    Hoch, J.A.3
  • 59
    • 70349764676 scopus 로고    scopus 로고
    • Structure of PAS-linked histidine kinase and the response regulator complex
    • Yamada S, Sugimoto H, Kobayashi M, Ohno A, Nakamura H, Shiro Y. 2009. Structure of PAS-linked histidine kinase and the response regulator complex. Structure 17:1333-1344. http://dx.doi.org/10.1016/j.str.2009.07.016.
    • (2009) Structure , vol.17 , pp. 1333-1344
    • Yamada, S.1    Sugimoto, H.2    Kobayashi, M.3    Ohno, A.4    Nakamura, H.5    Shiro, Y.6
  • 60
    • 0035170897 scopus 로고    scopus 로고
    • Competence modulation by the NADH oxidase of Streptococcus pneumoniae involves signal transduction
    • Echenique JR, Trombe MC. 2001. Competence modulation by the NADH oxidase of Streptococcus pneumoniae involves signal transduction. J. Bacteriol. 183:768-772. http://dx.doi.org/10.1128/JB.183.2.768-772.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 768-772
    • Echenique, J.R.1    Trombe, M.C.2
  • 61
    • 77951033959 scopus 로고    scopus 로고
    • Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain
    • Gutu AD, Wayne KJ, Sham LT, Winkler ME. 2010. Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain. J. Bacteriol. 192:2346-2358. http://dx.doi.org/10.1128/JB.01690-09.
    • (2010) J. Bacteriol. , vol.192 , pp. 2346-2358
    • Gutu, A.D.1    Wayne, K.J.2    Sham, L.T.3    Winkler, M.E.4
  • 63
    • 0028783371 scopus 로고
    • Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V
    • Swairjo MA, Concha NO, Kaetzel MA, Dedman JR, Seaton BA. 1995. Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nat. Struct. Biol. 2:968-974. http://dx.doi.org/10.1038/nsb1195-968.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 968-974
    • Swairjo, M.A.1    Concha, N.O.2    Kaetzel, M.A.3    Dedman, J.R.4    Seaton, B.A.5
  • 64
    • 0033744568 scopus 로고    scopus 로고
    • Opening of the active site of Clostridium perfringens alpha-toxin may be triggered by membrane binding
    • Titball RW, Naylor CE, Miller J, Moss DS, Basak AK. 2000. Opening of the active site of Clostridium perfringens alpha-toxin may be triggered by membrane binding. Int. J. Med. Microbiol. 290:357-361. http://dx.doi.org/10.1016/S1438-4221(00)80040-5.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 357-361
    • Titball, R.W.1    Naylor, C.E.2    Miller, J.3    Moss, D.S.4    Basak, A.K.5
  • 65
    • 36348940343 scopus 로고    scopus 로고
    • Transcript and protein level analyses of the interactions among PhoB, PhoR, PhoU and CreC in response to phosphate starvation in Escherichia coli
    • Baek JH, Kang YJ, Lee SY. 2007. Transcript and protein level analyses of the interactions among PhoB, PhoR, PhoU and CreC in response to phosphate starvation in Escherichia coli. FEMS Microbiol. Lett. 277:254-259. http://dx.doi.org/10.1111/j.1574-6968.2007.00965.x.
    • (2007) FEMS Microbiol. Lett. , vol.277 , pp. 254-259
    • Baek, J.H.1    Kang, Y.J.2    Lee, S.Y.3
  • 66
    • 80655125014 scopus 로고    scopus 로고
    • Twocomponent PhoB-PhoR regulatory system and ferric uptake regulator sense phosphate and iron to control virulence genes in type III and VI secretion systems of Edwardsiella tarda
    • Chakraborty S, Sivaraman J, Leung KY, Mok YK. 2011. Twocomponent PhoB-PhoR regulatory system and ferric uptake regulator sense phosphate and iron to control virulence genes in type III and VI secretion systems of Edwardsiella tarda. J. Biol. Chem. 286:39417-39430. http://dx.doi.org/10.1074/jbc.M111.295188.
    • (2011) J. Biol. Chem. , vol.286 , pp. 39417-39430
    • Chakraborty, S.1    Sivaraman, J.2    Leung, K.Y.3    Mok, Y.K.4
  • 67
    • 84880822645 scopus 로고    scopus 로고
    • The pathogenicity island encoded PvrSR/RcsCB regulatory network controls biofilm formation and dispersal in Pseudomonas aeruginosa PA14
    • Mikkelsen H, Hui K, Barraud N, Filloux A. 2013. The pathogenicity island encoded PvrSR/RcsCB regulatory network controls biofilm formation and dispersal in Pseudomonas aeruginosa PA14. Mol. Microbiol. 89: 450-463. http://dx.doi.org/10.1111/mmi.12287.
    • (2013) Mol. Microbiol. , vol.89 , pp. 450-463
    • Mikkelsen, H.1    Hui, K.2    Barraud, N.3    Filloux, A.4

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