메뉴 건너뛰기




Volumn 75, Issue , 2003, Pages 293-320

The Roles and Regulation of Potassium in Bacteria

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM; POTASSIUM CHANNEL;

EID: 1542570529     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6603(03)75008-9     Document Type: Review
Times cited : (405)

References (145)
  • 1
    • 4444339551 scopus 로고
    • Potassium transport in bacteria
    • M.O Walderhaug D.C Dosch W Epstein Potassium transport in bacteria B Rosen S Silver Ion Transport in Prokaryotes 1987 Academic Press New York 85 103
    • (1987) , pp. 85-103
    • Walderhaug, M.O1    Dosch, D.C2    Epstein, W3
  • 2
    • 0033022073 scopus 로고    scopus 로고
    • Bioenergetic aspects of halophilism
    • A Oren Bioenergetic aspects of halophilism Microbiol. Mol. Biol. Rev. 63 1999 334 348
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 334-348
    • Oren, A1
  • 3
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • D Madern C Ebel G Zaccai Halophilic adaptation of enzymes Extremophiles 4 2000 91 98
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D1    Ebel, C2    Zaccai, G3
  • 4
    • 85176182470 scopus 로고
    • A.D Brown Microbial Water Stress Physiology: Principles and Perspectives 1990 John Wiley Chichester
    • (1990)
    • Brown, A.D1
  • 5
    • 0025138269 scopus 로고
    • The surface stress theory for the case of Escherichia coli: the paradoxes of gram-negative growth
    • A.L Koch The surface stress theory for the case of Escherichia coli : the paradoxes of gram-negative growth Res. Microbiol. 141 1990 119 130
    • (1990) Res. Microbiol. , vol.141 , pp. 119-130
    • Koch, A.L1
  • 6
    • 0017703597 scopus 로고
    • Periplasmic space in Salmonella typhimurium and Escherichia coli
    • J.B Stock B Rausch S Roseman Periplasmic space in Salmonella typhimurium and Escherichia coli J. Biol. Chem. 252 1977 7850 7861
    • (1977) J. Biol. Chem. , vol.252 , pp. 7850-7861
    • Stock, J.B1    Rausch, B2    Roseman, S3
  • 7
    • 0034028431 scopus 로고    scopus 로고
    • Biophysical characterization of changes in the amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress
    • D.S Cayley H.J Guttman M.T Record Jr. Biophysical characterization of changes in the amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress Biophys. J. 78 2000 1748 1764
    • (2000) Biophys. J. , vol.78 , pp. 1748-1764
    • Cayley, D.S1    Guttman, H.J2    Record, M.T3
  • 8
    • 0005309866 scopus 로고
    • Osmotic and Donnan equilibriums in poly(acrylic acid)-sodium bromide solutions
    • S Alexandrowicz Osmotic and Donnan equilibriums in poly(acrylic acid)-sodium bromide solutions J. Poly. Sci. 56 1962 115 132
    • (1962) J. Poly. Sci. , vol.56 , pp. 115-132
    • Alexandrowicz, S1
  • 9
    • 0025695355 scopus 로고
    • Determination of turgor pressure in Bacillus subtilis: a possible role for K+ in turgor regulation
    • + in turgor regulation J. Gen. Microbiol. 136 1990 2521 2526
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 2521-2526
    • Whatmore, A.M1    Reed, R.H2
  • 10
    • 85010292860 scopus 로고    scopus 로고
    • The biophysics of the gram-negative periplasmic space
    • A.L Koch The biophysics of the gram-negative periplasmic space Crit. Rev. Microbiol. 24 1998 23 59
    • (1998) Crit. Rev. Microbiol. , vol.24 , pp. 23-59
    • Koch, A.L1
  • 11
    • 85005627207 scopus 로고
    • Cation transport in Escherichia coli. V. Regulation of cation content
    • W Epstein S.G Schultz Cation transport in Escherichia coli . V. Regulation of cation content J. Gen. Physiol. 49 1965 221 234
    • (1965) J. Gen. Physiol. , vol.49 , pp. 221-234
    • Epstein, W1    Schultz, S.G2
  • 12
    • 0023219316 scopus 로고
    • Replacement of potassium chloride by potassium glutamate dramatically enhances protein-DNA interactions in vitro
    • S Leirmo C Harrison D.S Cayler R.R Burgess M.T Record Jr. Replacement of potassium chloride by potassium glutamate dramatically enhances protein-DNA interactions in vitro Biochemistry 26 1987 7157 7164
    • (1987) Biochemistry , vol.26 , pp. 7157-7164
    • Leirmo, S1    Harrison, C2    Cayler, D.S3    Burgess, R.R4    Record, M.T5
  • 13
    • 0017276787 scopus 로고
    • Cation transport in Escherichia coli. VIII. Potassium transport mutants
    • D.B Rhoads F.B Waters W Epstein Cation transport in Escherichia coli . VIII. Potassium transport mutants J. Gen. Physiol. 67 1976 325 341
    • (1976) J. Gen. Physiol. , vol.67 , pp. 325-341
    • Rhoads, D.B1    Waters, F.B2    Epstein, W3
  • 14
    • 13444249326 scopus 로고
    • Cation transport in Escherichia coli. IV. Kinetics of net K uptake
    • S.G Schultz W Epstein A.K Solomon Cation transport in Escherichia coli. IV. Kinetics of net K uptake J. Gen. Physiol. 47 1963 329 346
    • (1963) J. Gen. Physiol. , vol.47 , pp. 329-346
    • Schultz, S.G1    Epstein, W2    Solomon, A.K3
  • 15
    • 0019786539 scopus 로고
    • Interconversion of components of the bacterial proton motive force by electrogenic potassium transport
    • E.P Bakker W.E Mangerich Interconversion of components of the bacterial proton motive force by electrogenic potassium transport J. Bacteriol. 147 1981 820 826
    • (1981) J. Bacteriol. , vol.147 , pp. 820-826
    • Bakker, E.P1    Mangerich, W.E2
  • 16
    • 0034108217 scopus 로고    scopus 로고
    • Rapid inactivation of the Escherichia coli Kdp K+ uptake system by high potassium concentrations
    • + uptake system by high potassium concentrations Mol. Microbiol. 35 2000 1235 1243
    • (2000) Mol. Microbiol. , vol.35 , pp. 1235-1243
    • Roe, A.J1    McLaggan, D2    O'Byrne, C.P3    Booth, I.R4
  • 17
    • 0015489101 scopus 로고
    • Cation transport and electrogenesis by Streptococcus faecalis
    • F.M Harold D Papineau Cation transport and electrogenesis by Streptococcus faecalis J. Membr. Biol. 8 1972 27 44
    • (1972) J. Membr. Biol. , vol.8 , pp. 27-44
    • Harold, F.M1    Papineau, D2
  • 18
    • 0023405086 scopus 로고
    • Low-affinity potassium uptake system in Bacillus acidocaldarius
    • M Michels E.P Bakker Low-affinity potassium uptake system in Bacillus acidocaldarius J. Bacteriol. 169 1987 4335 4341
    • (1987) J. Bacteriol. , vol.169 , pp. 4335-4341
    • Michels, M1    Bakker, E.P2
  • 19
    • 0037312744 scopus 로고    scopus 로고
    • KtrAB and KtrCD: two K+-uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity
    • +-uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity J. Bacteriol. 185 2003 1289 1298
    • (2003) J. Bacteriol. , vol.185 , pp. 1289-1298
    • Holtmann, G1    Bakker, E.P2    Uozumi, N3    Bremer, E4
  • 20
    • 0015155178 scopus 로고
    • Potassium transport loci in Escherichia coli K-12
    • W Epstein B.S Kim Potassium transport loci in Escherichia coli K-12 J. Bacteriol. 108 1971 639 644
    • (1971) J. Bacteriol. , vol.108 , pp. 639-644
    • Epstein, W1    Kim, B.S2
  • 21
    • 0026098110 scopus 로고
    • Genetic analysis of potassium transport loci in Escherichia coli: evidence for three constitutive systems mediating uptake of potassium
    • D.C Dosch G.L Helmer S.H Sutton F.F Salvacion W Epstein Genetic analysis of potassium transport loci in Escherichia coli : evidence for three constitutive systems mediating uptake of potassium J. Bacteriol. 173 1991 687 696
    • (1991) J. Bacteriol. , vol.173 , pp. 687-696
    • Dosch, D.C1    Helmer, G.L2    Sutton, S.H3    Salvacion, F.F4    Epstein, W5
  • 22
    • 0027934102 scopus 로고
    • A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium
    • C Parra-Lopez R Lin A Aspedon E.A Groisman A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium EMBO J. 13 1994 3964 3972
    • (1994) EMBO J. , vol.13 , pp. 3964-3972
    • Parra-Lopez, C1    Lin, R2    Aspedon, A3    Groisman, E.A4
  • 23
    • 0024447794 scopus 로고
    • K+-Transport protein TrkA of Escherichia coli is a peripheral membrane protein that requires other trk gene products for attachment to the cytoplasmatic membrane
    • +-Transport protein TrkA of Escherichia coli is a peripheral membrane protein that requires other trk gene products for attachment to the cytoplasmatic membrane J. Biol. Chem. 264 1989 16403 16410
    • (1989) J. Biol. Chem. , vol.264 , pp. 16403-16410
    • Bossemeyer, D1    Borchard, A2    Dosch, D.C3    Helmer, G.C4    Epstein, W5    Booth, I.R6    Bakker, E.P7
  • 25
    • 0027445662 scopus 로고
    • Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium
    • C Parra-Lopez M.T Baer E.A Groisman Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium EMBO J. 12 1993 4053 4062
    • (1993) EMBO J. , vol.12 , pp. 4053-4062
    • Parra-Lopez, C1    Baer, M.T2    Groisman, E.A3
  • 26
    • 0030933618 scopus 로고    scopus 로고
    • Requirement for a large K+ uptake capacity and of extracytoplasmic protease activity for protamine resistance of Escherichia coli
    • + uptake capacity and of extracytoplasmic protease activity for protamine resistance of Escherichia coli Arch. Microbiol. 167 1997 126 136
    • (1997) Arch. Microbiol. , vol.167 , pp. 126-136
    • Stumpe, S1    Bakker, E.P2
  • 27
    • 0028969793 scopus 로고
    • TrkH and its homolog, TrkG, determine the specificity and kinetics of cation transport by the Trk system of Escherichia coli
    • A Schlösser M.W Meldorf S Stumpe E.P Bakker W Epstein TrkH and its homolog, TrkG, determine the specificity and kinetics of cation transport by the Trk system of Escherichia coli J. Bacteriol. 177 1995 1908 1910
    • (1995) J. Bacteriol. , vol.177 , pp. 1908-1910
    • Schlösser, A1    Meldorf, M.W2    Stumpe, S3    Bakker, E.P4    Epstein, W5
  • 30
    • 49049126211 scopus 로고
    • pH-dependent transport of rubidium by the constitutive potassium transport system TrkA of Escherichia coli
    • E Bakker pH-dependent transport of rubidium by the constitutive potassium transport system TrkA of Escherichia coli FEMS Micro. Lett. 16 1983 229 233
    • (1983) FEMS Micro. Lett. , vol.16 , pp. 229-233
    • Bakker, E1
  • 31
    • 0017360007 scopus 로고
    • Energy coupling to net K+-transport in Escherichia coli K-12
    • +-transport in Escherichia coli K-12 J. Biol. Chem. 252 1977 1394 1401
    • (1977) J. Biol. Chem. , vol.252 , pp. 1394-1401
    • Rhoads, D.B1    Epstein, W2
  • 32
    • 0021993020 scopus 로고
    • Energy coupling to K+ uptake via the Trk system of Escherichia coli: the role of ATP
    • + uptake via the Trk system of Escherichia coli : the role of ATP J. Gen. Microbiol. 131 1985 77 85
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 77-85
    • Stewart, L.M.D1    Bakker, E.P2    Booth, I.R3
  • 34
    • 0025897380 scopus 로고
    • Subcloning, nucleotide sequence and expression of trkG, a gene that encodes an integral membrane protein involved in potassium uptake via the Trk system of Escherichia coli
    • A Schlösser S Kluttig A Hamann E.P Bakker Subcloning, nucleotide sequence and expression of trkG , a gene that encodes an integral membrane protein involved in potassium uptake via the Trk system of Escherichia coli J. Bacteriol. 173 1991 3170 3176
    • (1991) J. Bacteriol. , vol.173 , pp. 3170-3176
    • Schlösser, A1    Kluttig, S2    Hamann, A3    Bakker, E.P4
  • 36
    • 0017807533 scopus 로고
    • Potassium uniport and ATP synthesis in Halobacterium halobium
    • G Wagner R Hartmann D Oesterhelt Potassium uniport and ATP synthesis in Halobacterium halobium Eur. J. Biochem. 89 1978 169 179
    • (1978) Eur. J. Biochem. , vol.89 , pp. 169-179
    • Wagner, G1    Hartmann, R2    Oesterhelt, D3
  • 37
    • 0010704785 scopus 로고
    • ATP is required for K+ active transport in the archaebacterium Haloferax volcanii
    • + active transport in the archaebacterium Haloferax volcanii Arch. Microbiol. 151 1989 530 536
    • (1989) Arch. Microbiol. , vol.151 , pp. 530-536
    • Meury, J1    Kohiyama, M2
  • 39
    • 0032921035 scopus 로고    scopus 로고
    • Change to alanine of one out of four selectivity filter glycines in KtrB causes a two order of magnitude decrease in the affinities for both K+ and Na+ of the Na+ dependent K+ uptake system KtrAB from Vibrio alginolyticus
    • + uptake system KtrAB from Vibrio alginolyticus FEMS Lett. 450 1999 217 220
    • (1999) FEMS Lett. , vol.450 , pp. 217-220
    • Tholema, N1    Bakker, E.P2    Suzuki, A3    Nakamura, T4
  • 40
    • 0037077136 scopus 로고    scopus 로고
    • A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch
    • T.P Roosild S Miller I.R Booth S Choe A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch Cell 109 2002 781 791
    • (2002) Cell , vol.109 , pp. 781-791
    • Roosild, T.P1    Miller, S2    Booth, I.R3    Choe, S4
  • 41
    • 0033055580 scopus 로고    scopus 로고
    • Two major potassium uptake systems, KtrI and KtrII, in Enterococcus hirae
    • M Kawano K Igarashi Y Kakinuma Two major potassium uptake systems, KtrI and KtrII, in Enterococcus hirae FEMS Microbiol. Lett. 176 1999 449 453
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 449-453
    • Kawano, M1    Igarashi, K2    Kakinuma, Y3
  • 42
    • 0018885437 scopus 로고
    • Energy coupling to potassium transport in Streptococcus fecalis: interplay of ATP and the protonmotive force
    • E.P Bakker F.M Harold Energy coupling to potassium transport in Streptococcus fecalis : interplay of ATP and the protonmotive force J. Biol. Chem. 255 1980 433 440
    • (1980) J. Biol. Chem. , vol.255 , pp. 433-440
    • Bakker, E.P1    Harold, F.M2
  • 43
    • 77957093882 scopus 로고    scopus 로고
    • The Kdp-ATPase of Escherichia coli
    • K Altendorf W Epstein The Kdp-ATPase of Escherichia coli A.G Lee Biomembranes V 1996 JAL Press Greenwich 403 420
    • (1996) , pp. 403-420
    • Altendorf, K1    Epstein, W2
  • 45
    • 0019411090 scopus 로고
    • Uptake of potassium and rubidium ions by the cyanobacterium Anabaena variabilis
    • R.H Reed P Rowell W.D.P Stewart Uptake of potassium and rubidium ions by the cyanobacterium Anabaena variabilis FEMS Microbiol. Lett. 11 1981 233 236
    • (1981) FEMS Microbiol. Lett. , vol.11 , pp. 233-236
    • Reed, R.H1    Rowell, P2    Stewart, W.D.P3
  • 46
    • 0022386602 scopus 로고
    • K+-ATPase from Rhizobium sp. UMKL 20
    • +-ATPase from Rhizobium sp. UMKL 20 Arch. Microbiol. 142 1985 393 396
    • (1985) Arch. Microbiol. , vol.142 , pp. 393-396
    • Lim, S.T1
  • 47
    • 0342546514 scopus 로고    scopus 로고
    • The KdpF subunit is part of the K+-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro
    • +-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro J. Biol. Chem. 274 1999 37901 37907
    • (1999) J. Biol. Chem. , vol.274 , pp. 37901-37907
    • Gassel, M1    Mollenkamp, T2    Puppe, W3    Altendorf, K4
  • 48
    • 0028910065 scopus 로고
    • Genetic evidence for two sequentially occupied K+ binding sites in the Kdp transport ATPase
    • + binding sites in the Kdp transport ATPase J. Biol. Chem. 270 1995 6678 6685
    • (1995) J. Biol. Chem. , vol.270 , pp. 6678-6685
    • Buurman, E.T1    Kim, K.-T2    Epstein, W3
  • 49
    • 0035971178 scopus 로고    scopus 로고
    • Substrate-binding clusters of the K+-transporting Kdp ATPase of Escherichia coli investigated by amber suppression scanning mutagenesis
    • +-transporting Kdp ATPase of Escherichia coli investigated by amber suppression scanning mutagenesis J. Biol. Chem. 276 2001 9590 9598
    • (2001) J. Biol. Chem. , vol.276 , pp. 9590-9598
    • Dorus, S1    Mimura, H2    Epstein, W3
  • 52
    • 0029977452 scopus 로고    scopus 로고
    • Electrogenic transport by the Kdp-ATPase of Escherichia coli
    • K Fendler S Dröse K Altendorf E Bamberg Electrogenic transport by the Kdp-ATPase of Escherichia coli Biochemistry 35 1996 8009 8017
    • (1996) Biochemistry , vol.35 , pp. 8009-8017
    • Fendler, K1    Dröse, S2    Altendorf, K3    Bamberg, E4
  • 54
    • 0033010261 scopus 로고    scopus 로고
    • Kup is the major K+ uptake system in Escherichia coli upon hyperosmotic stress at low pH
    • + uptake system in Escherichia coli upon hyperosmotic stress at low pH FEBS Lett. 447 1999 144 148
    • (1999) FEBS Lett. , vol.447 , pp. 144-148
    • Trchounian, A1    Kobayashi, H2
  • 55
    • 0027520486 scopus 로고
    • Nucleotide sequence and 3′-end deletion studies indicate that the K+-uptake protein Kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus
    • +-uptake protein Kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus J. Bacteriol. 175 1993 6925 6931
    • (1993) J. Bacteriol. , vol.175 , pp. 6925-6931
    • Schleyer, M1    Bakker, E.P2
  • 56
    • 0021689497 scopus 로고
    • Tetracycline resistance element of pBR322 mediates potassium transport
    • D.C Dosch F.F Salvacion W Epstein Tetracycline resistance element of pBR322 mediates potassium transport J. Bacteriol. 160 1984 1188 1190
    • (1984) J. Bacteriol. , vol.160 , pp. 1188-1190
    • Dosch, D.C1    Salvacion, F.F2    Epstein, W3
  • 57
    • 0031061537 scopus 로고
    • Diverse genes of the alkaliphilic Bacillus firmus OF4 that complement K+-uptake-deficient Escherichia coli including an ftsH homologue
    • +-uptake-deficient Escherichia coli including an ftsH homologue Extremophiles 1 1995 22 28
    • (1995) Extremophiles , vol.1 , pp. 22-28
    • Ito, M1    Cooperberg, B2    Krulwich, T.A3
  • 58
    • 0036651823 scopus 로고    scopus 로고
    • Isolation of Enterococcus hirae mutant deficient in low-affinity potassium uptake at alkaline pH
    • M Kawano K Igarashi Y Kakinuma Isolation of Enterococcus hirae mutant deficient in low-affinity potassium uptake at alkaline pH Biosci. Biotechnol. Biochem. 66 2002 1597 1600
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1597-1600
    • Kawano, M1    Igarashi, K2    Kakinuma, Y3
  • 59
    • 0032500617 scopus 로고    scopus 로고
    • Electrogenic antiport activities of the Gram-positive Tet proteins include a Na+(K+)/K+ mode that mediates net K+ uptake
    • + uptake J. Biol. Chem. 273 1998 26447 26454
    • (1998) J. Biol. Chem. , vol.273 , pp. 26447-26454
    • Guffanti, A.A1    Cheng, J2    Krulwich, T.A3
  • 61
    • 0034110783 scopus 로고    scopus 로고
    • Two types of Bacillus subtilis tetA(L) deletion strains reveal the physiological importance of TetA(L) in K+ acquisition as well as in Na+, alkali and tetracycline resistance
    • +, alkali and tetracycline resistance J. Bacteriol. 182 2000 2088 2095
    • (2000) J. Bacteriol. , vol.182 , pp. 2088-2095
    • Wang, W1    Guffanti, A.A2    Wei, Y3    Ito, M4    Krulwich, T.A5
  • 63
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism
    • P Mitchell Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism Nature 191 1961 144 148
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P1
  • 66
    • 0033151720 scopus 로고    scopus 로고
    • Protective mechanisms against toxic electrophiles in Escherichia coli
    • G.P Ferguson Protective mechanisms against toxic electrophiles in Escherichia coli Trends Microbiol. 7 1999 242 247
    • (1999) Trends Microbiol. , vol.7 , pp. 242-247
    • Ferguson, G.P1
  • 67
    • 0019274593 scopus 로고
    • Opening of potassium channels in Escherichia coli membranes by thiol reagents and the recovery of potassium tightness
    • J Meury S Lebail A Kepes Opening of potassium channels in Escherichia coli membranes by thiol reagents and the recovery of potassium tightness Eur. J. Biochem. 113 1980 33 38
    • (1980) Eur. J. Biochem. , vol.113 , pp. 33-38
    • Meury, J1    Lebail, S2    Kepes, A3
  • 68
    • 0020337792 scopus 로고
    • Glutathione and the gated potassium channels of Escherichia coli
    • J Meury A Kepes Glutathione and the gated potassium channels of Escherichia coli EMBO J. 1 1982 339 343
    • (1982) EMBO J. , vol.1 , pp. 339-343
    • Meury, J1    Kepes, A2
  • 69
    • 0019952705 scopus 로고
    • N-ethylmaleimide induces K+-H+ antiport activity in Escherichia coli K-12
    • + antiport activity in Escherichia coli K-12 FEBS Lett. 140 1982 177 180
    • (1982) FEBS Lett. , vol.140 , pp. 177-180
    • Bakker, E.P1    Mangerich, W.E2
  • 70
    • 0026036336 scopus 로고
    • The cloning and DNA sequence of the gene for the glutathione-regulated potassium-efflux system KefC of Escherichia coli
    • A.W Munro G.Y Ritchie A.J Lamb R.M Douglas I.R Booth The cloning and DNA sequence of the gene for the glutathione-regulated potassium-efflux system KefC of Escherichia coli Mol. Microbiol. 5 1991 607 616
    • (1991) Mol. Microbiol. , vol.5 , pp. 607-616
    • Munro, A.W1    Ritchie, G.Y2    Lamb, A.J3    Douglas, R.M4    Booth, I.R5
  • 71
    • 0033765070 scopus 로고    scopus 로고
    • Identification of an ancillary protein, YapF, required for the activity of the KefC glutathione-gated potassium efflux system in Escherichia coli
    • S Miller L.S Ness C.M Wood B.C Fox I.R Booth Identification of an ancillary protein, YapF, required for the activity of the KefC glutathione-gated potassium efflux system in Escherichia coli J. Bacteriol. 182 2000 6536 6540
    • (2000) J. Bacteriol. , vol.182 , pp. 6536-6540
    • Miller, S1    Ness, L.S2    Wood, C.M3    Fox, B.C4    Booth, I.R5
  • 72
    • 0018840160 scopus 로고
    • Cation/proton antiport systems in Escherichia coli: properties of the potassium/proton antiporter
    • R.N Brey B.P Rosen E.N Sorensen Cation/proton antiport systems in Escherichia coli : properties of the potassium/proton antiporter J. Biol. Chem. 255 1980 39 44
    • (1980) J. Biol. Chem. , vol.255 , pp. 39-44
    • Brey, R.N1    Rosen, B.P2    Sorensen, E.N3
  • 73
    • 0018875653 scopus 로고
    • Cation/proton antiport systems in Escherichia coli: absence of potassium/proton antiporter activity in a pH-sensitive mutant
    • B.P Plack Jr. R.H Rosen Cation/proton antiport systems in Escherichia coli : absence of potassium/proton antiporter activity in a pH-sensitive mutant J. Biol. Chem. 255 1980 3824 3825
    • (1980) J. Biol. Chem. , vol.255 , pp. 3824-3825
    • Plack, B.P1    Rosen, R.H2
  • 74
    • 0032988015 scopus 로고    scopus 로고
    • Isolation and properties of Enterococcus hirae mutants defective in the potassium/proton antiport system
    • Y Kakinuma K Igarashi Isolation and properties of Enterococcus hirae mutants defective in the potassium/proton antiport system J. Bacteriol. 181 1999 4103 4105
    • (1999) J. Bacteriol. , vol.181 , pp. 4103-4105
    • Kakinuma, Y1    Igarashi, K2
  • 76
    • 0021875793 scopus 로고
    • Characterization of ammonium (methylammonium)/potassium antiport in Escherichia coli
    • A Jayakumar W Epstein E.M Barnes Jr. Characterization of ammonium (methylammonium)/potassium antiport in Escherichia coli J. Biol. Chem. 260 1985 7528 7532
    • (1985) J. Biol. Chem. , vol.260 , pp. 7528-7532
    • Jayakumar, A1    Epstein, W2    Barnes, E.M3
  • 77
    • 0021748004 scopus 로고
    • Ammonia/potassium exchange in methanogenic bacteria
    • G.D Sprott K.M Shaw K.F Jarrell Ammonia/potassium exchange in methanogenic bacteria J. Biol. Chem. 259 1984 12602 12608
    • (1984) J. Biol. Chem. , vol.259 , pp. 12602-12608
    • Sprott, G.D1    Shaw, K.M2    Jarrell, K.F3
  • 78
    • 85176158780 scopus 로고    scopus 로고
    • Bacterial channels
    • I.R Booth Bacterial channels J.K Setlow Genetic Engineering XXV 2003 Kluwer Academic/Plenum Publishing New York 91 111
    • (2003) , pp. 91-111
    • Booth, I.R1
  • 80
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Y Jiang A Lee J Chen M Cadene B.T Chait R MacKinnon Crystal structure and mechanism of a calcium-gated potassium channel Nature 417 2002 515 522
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y1    Lee, A2    Chen, J3    Cadene, M4    Chait, B.T5    MacKinnon, R6
  • 82
    • 0028222121 scopus 로고
    • An Escherichia coli homologue of eucaryotic potassium channel proteins
    • R Milkman An Escherichia coli homologue of eucaryotic potassium channel proteins Proc. Natl. Acad. Sci. USA 91 1994 3510 3514
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3510-3514
    • Milkman, R1
  • 84
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel
    • G Chang R.H Spencer A.T Lee M.T Barclay D.C Rees Structure of the MscL homolog from Mycobacterium tuberculosis : a gated mechanosensitive ion channel Science 282 1998 2220 2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G1    Spencer, R.H2    Lee, A.T3    Barclay, M.T4    Rees, D.C5
  • 85
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • R.B Bass P Strop M Barclay D.C Rees Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel Science 298 2002 1582 1587
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B1    Strop, P2    Barclay, M3    Rees, D.C4
  • 86
    • 0037107398 scopus 로고    scopus 로고
    • Ionic regulation of MscK, a mechanosensitive channel from Escherichia coli
    • Y Li P.C Moe S Chandrasekaran I.R Booth P Blount Ionic regulation of MscK, a mechanosensitive channel from Escherichia coli EMBO J. 21 2002 1 8
    • (2002) EMBO J. , vol.21 , pp. 1-8
    • Li, Y1    Moe, P.C2    Chandrasekaran, S3    Booth, I.R4    Blount, P5
  • 87
    • 0029928179 scopus 로고    scopus 로고
    • Effect of mutation of potassium-efflux system, KefA, on mechanosensitive channels in the cytoplasmic membrane of Escherichia coli
    • C Cui J Adler Effect of mutation of potassium-efflux system, KefA, on mechanosensitive channels in the cytoplasmic membrane of Escherichia coli J. Membr. Biol. 150 1996 143 152
    • (1996) J. Membr. Biol. , vol.150 , pp. 143-152
    • Cui, C1    Adler, J2
  • 88
    • 0036169863 scopus 로고    scopus 로고
    • Analysis of the kefA2 mutation suggests that KefA is a cation-specific channel involved in osmotic adaptation in Escherichia coli
    • D McLaggan M.A Jones G Gouesbet N Levina S Lindey W Epstein I.R Booth Analysis of the kefA2 mutation suggests that KefA is a cation-specific channel involved in osmotic adaptation in Escherichia coli Mol. Microbiol. 43 2002 521 536
    • (2002) Mol. Microbiol. , vol.43 , pp. 521-536
    • McLaggan, D1    Jones, M.A2    Gouesbet, G3    Levina, N4    Lindey, S5    Epstein, W6    Booth, I.R7
  • 89
    • 0026525773 scopus 로고
    • Gadolinium ion inhibits loss of metabolites induced by osmotic shock and large stretch-activated channels in bacteria
    • C.A Berrier A Coulombe I Szabó M Zoratti A Ghazi Gadolinium ion inhibits loss of metabolites induced by osmotic shock and large stretch-activated channels in bacteria Eur. J. Biochem. 206 1992 559 565
    • (1992) Eur. J. Biochem. , vol.206 , pp. 559-565
    • Berrier, C.A1    Coulombe, A2    Szabó, I3    Zoratti, M4    Ghazi, A5
  • 90
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of the MscS and MscL mechanosensitive channels: identification of the genes required for MscS activity
    • N Levina S Tötemeyer N.R Stokes P Louis M.A Jones I.R Booth Protection of Escherichia coli cells against extreme turgor by activation of the MscS and MscL mechanosensitive channels: identification of the genes required for MscS activity EMBO J. 18 1999 1730 1737
    • (1999) EMBO J. , vol.18 , pp. 1730-1737
    • Levina, N1    Tötemeyer, S2    Stokes, N.R3    Louis, P4    Jones, M.A5    Booth, I.R6
  • 91
    • 84979136982 scopus 로고
    • Experiments in active and passive permeability of Bacillus coli communis
    • S.L Ørskov Experiments in active and passive permeability of Bacillus coli communis Acta Path. Microbiol. Scand. 25 1948 277 283
    • (1948) Acta Path. Microbiol. Scand. , vol.25 , pp. 277-283
    • Ørskov, S.L1
  • 92
    • 0017823251 scopus 로고
    • Cation transport in Escherichia coli. IX. Regulation of K+ transport
    • + transport J. Gen. Physiol. 72 1978 283 295
    • (1978) J. Gen. Physiol. , vol.72 , pp. 283-295
    • Rhoads, D.B1    Epstein, W2
  • 93
    • 0000341849 scopus 로고
    • Ionic osmoregulation during salt adaptation of the cyanobacterium Synechococcus 6311
    • E Blumwald R.J Mehlhorn L Packer Ionic osmoregulation during salt adaptation of the cyanobacterium Synechococcus 6311 Plant Physiol. 73 1983 377 380
    • (1983) Plant Physiol. , vol.73 , pp. 377-380
    • Blumwald, E1    Mehlhorn, R.J2    Packer, L3
  • 94
    • 0025674148 scopus 로고
    • The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis
    • A.M Whatmore J.A Chudek R.H Reed The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis J. Gen. Microbiol. 136 1990 2527 2535
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 2527-2535
    • Whatmore, A.M1    Chudek, J.A2    Reed, R.H3
  • 96
    • 0035477802 scopus 로고    scopus 로고
    • The osmoreactive betaine carrier BetP from Corynebacterium glutamicum is a sensor for cytoplasmic K+
    • + EMBO J. 20 2001 5412 5420
    • (2001) EMBO J. , vol.20 , pp. 5412-5420
    • Rübenhagen, R1    Morbach, S2    Krämer, R3
  • 97
    • 0034669780 scopus 로고    scopus 로고
    • Switching osmolyte strategies: response of Methanococcus thermolithotrophicus to changes in external NaCl
    • D.D Martin R.A Ciulla P.M Robinson M.F Roberts Switching osmolyte strategies: response of Methanococcus thermolithotrophicus to changes in external NaCl Biochim. Biophys. Acta 1524 2000 1 10
    • (2000) Biochim. Biophys. Acta , vol.1524 , pp. 1-10
    • Martin, D.D1    Ciulla, R.A2    Robinson, P.M3    Roberts, M.F4
  • 98
    • 0022610802 scopus 로고
    • Osmoregulation by potassium transport in Escherichia coli
    • W Epstein Osmoregulation by potassium transport in Escherichia coli FEMS Microbiol. Rev. 39 1986 73 78
    • (1986) FEMS Microbiol. Rev. , vol.39 , pp. 73-78
    • Epstein, W1
  • 99
    • 0020534963 scopus 로고
    • The effects of weak acids on potassium uptake by Escherichia coli K-12. Inhibition by low cytoplasmic pH
    • E.P Bakker W.E Mangerich The effects of weak acids on potassium uptake by Escherichia coli K-12. Inhibition by low cytoplasmic pH Biochim. Biophys. Acta 730 1983 379 386
    • (1983) Biochim. Biophys. Acta , vol.730 , pp. 379-386
    • Bakker, E.P1    Mangerich, W.E2
  • 100
    • 0030903288 scopus 로고    scopus 로고
    • Characterization of transcriptional regulation of the kdp operon of Salmonella typhimurium
    • J.S Frymier T.D Reed S.A Fletcher L.N Csonka Characterization of transcriptional regulation of the kdp operon of Salmonella typhimurium J. Bacteriol. 179 1997 3061 3063
    • (1997) J. Bacteriol. , vol.179 , pp. 3061-3063
    • Frymier, J.S1    Reed, T.D2    Fletcher, S.A3    Csonka, L.N4
  • 101
    • 0033981568 scopus 로고    scopus 로고
    • Protection of the DNA during exposure of Escherichia coli cells to a toxic metabolite: the role of the KefB and KefC potassium channels
    • G.P Ferguson J.R Battista A.T Lee I.R Booth Protection of the DNA during exposure of Escherichia coli cells to a toxic metabolite: the role of the KefB and KefC potassium channels Mol. Microbiol. 35 2000 113 122
    • (2000) Mol. Microbiol. , vol.35 , pp. 113-122
    • Ferguson, G.P1    Battista, J.R2    Lee, A.T3    Booth, I.R4
  • 102
    • 0030759181 scopus 로고    scopus 로고
    • Mutations in the glutathione-gated KefC K+ efflux system of Escherichia coli that cause constitutive activation
    • + efflux system of Escherichia coli that cause constitutive activation J. Biol. Chem. 272 1997 24942 24947
    • (1997) J. Biol. Chem. , vol.272 , pp. 24942-24947
    • Miller, S1    Douglas, R.M2    Carter, P3    Booth, I.R4
  • 103
    • 0011100093 scopus 로고
    • Osmotic control of kdp operon expression in Escherichia coli
    • L.A Laimins D.B Rhoads W Epstein Osmotic control of kdp operon expression in Escherichia coli Proc. Natl. Acad. Sci. USA 78 1981 464 468
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 464-468
    • Laimins, L.A1    Rhoads, D.B2    Epstein, W3
  • 104
    • 0023407982 scopus 로고
    • High-affinity potassium uptake system in Bacillus acidocaldarius showing immunological cross-reactivity with the Kdp system from Escherichia coli
    • E.P Bakker A Borchard M Michels K Altendorf A Siebers High-affinity potassium uptake system in Bacillus acidocaldarius showing immunological cross-reactivity with the Kdp system from Escherichia coli J. Bacteriol. 169 1987 4342 4348
    • (1987) J. Bacteriol. , vol.169 , pp. 4342-4348
    • Bakker, E.P1    Borchard, A2    Michels, M3    Altendorf, K4    Siebers, A5
  • 105
    • 0024645020 scopus 로고
    • The high-affinity K+-translocating ATPase complex from Bacillus acidocaldarius consists of three subunits
    • +-translocating ATPase complex from Bacillus acidocaldarius consists of three subunits Mol. Microbiol. 3 1989 487 495
    • (1989) Mol. Microbiol. , vol.3 , pp. 487-495
    • Hafer, J1    Siebers, A2    Bakker, E.P3
  • 106
    • 0030806964 scopus 로고    scopus 로고
    • The kdp system of Clostridium acetobutylicum: cloning, sequencing, and transcriptional regulation in response to potassium concentration
    • A Treuner-Lange A Kuhn P Durre The kdp system of Clostridium acetobutylicum : cloning, sequencing, and transcriptional regulation in response to potassium concentration J. Bacteriol. 179 1997 4501 4512
    • (1997) J. Bacteriol. , vol.179 , pp. 4501-4512
    • Treuner-Lange, A1    Kuhn, A2    Durre, P3
  • 107
    • 0034801549 scopus 로고    scopus 로고
    • Regulation of potassium-dependent Kdp-ATPase expression in the nitrogen-fixing cyanobacterium Anabaena torulosa
    • A Alahari A Ballal S Apte Regulation of potassium-dependent Kdp-ATPase expression in the nitrogen-fixing cyanobacterium Anabaena torulosa J. Bacteriol. 183 2001 5778 5781
    • (2001) J. Bacteriol. , vol.183 , pp. 5778-5781
    • Alahari, A1    Ballal, A2    Apte, S3
  • 108
    • 0026544871 scopus 로고
    • KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators
    • M.O Walderhaug J.W Polarek P Voelkner J.M Daniel J.E Hesse K Altendorf W Epstein KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators J. Bacteriol. 174 1992 2152 2159
    • (1992) J. Bacteriol. , vol.174 , pp. 2152-2159
    • Walderhaug, M.O1    Polarek, J.W2    Voelkner, P3    Daniel, J.M4    Hesse, J.E5    Altendorf, K6    Epstein, W7
  • 109
    • 0036318758 scopus 로고    scopus 로고
    • A chimeric Anabaena/Escherichia coli KdpD protein (Anacoli KdpD) functionally interacts with E. coli KdpE and activates kdp expression in E. coli
    • A Ballal R Heermann K Jung M Gassel S.K Apte K Altendorf A chimeric Anabaena/Escherichia coli KdpD protein (Anacoli KdpD) functionally interacts with E. coli KdpE and activates kdp expression in E. coli Arch. Microbiol. 178 2002 141 148
    • (2002) Arch. Microbiol. , vol.178 , pp. 141-148
    • Ballal, A1    Heermann, R2    Jung, K3    Gassel, M4    Apte, S.K5    Altendorf, K6
  • 110
    • 0034595636 scopus 로고    scopus 로고
    • The hydrophilic N-terminal domain complements the membrane-anchored C-terminal domain of the sensor kinase KdpD of Escherichia coli
    • R Heermann K Altendorf K Jung The hydrophilic N-terminal domain complements the membrane-anchored C-terminal domain of the sensor kinase KdpD of Escherichia coli J. Biol. Chem. 275 2000 17080 17085
    • (2000) J. Biol. Chem. , vol.275 , pp. 17080-17085
    • Heermann, R1    Altendorf, K2    Jung, K3
  • 111
    • 0028856709 scopus 로고
    • Membrane topology analysis of the sensor kinase KdpD of Escherichia coli
    • P Zimmann W Puppe K Altendorf Membrane topology analysis of the sensor kinase KdpD of Escherichia coli J. Biol. Chem. 270 1995 28282 28288
    • (1995) J. Biol. Chem. , vol.270 , pp. 28282-28288
    • Zimmann, P1    Puppe, W2    Altendorf, K3
  • 112
    • 0032500535 scopus 로고    scopus 로고
    • Individual substitutions of clustered arginine residues of the sensor kinase KdpD of Escherichia coli modulate the ratio of kinase to phosphatase activity
    • K Jung K Altendorf Individual substitutions of clustered arginine residues of the sensor kinase KdpD of Escherichia coli modulate the ratio of kinase to phosphatase activity J. Biol. Chem. 273 1998 26415 26420
    • (1998) J. Biol. Chem. , vol.273 , pp. 26415-26420
    • Jung, K1    Altendorf, K2
  • 113
    • 0032449734 scopus 로고    scopus 로고
    • The turgor sensor KdpD of Escherichia coli is a homodimer
    • R Heermann K Altendorf K Jung The turgor sensor KdpD of Escherichia coli is a homodimer Biochim. Biophys. Acta 1415 1998 114 124
    • (1998) Biochim. Biophys. Acta , vol.1415 , pp. 114-124
    • Heermann, R1    Altendorf, K2    Jung, K3
  • 114
    • 0036195846 scopus 로고    scopus 로고
    • Towards an understanding of the molecular mechanisms of stimulus perception and signal transduction by the KdpD/KdpE system of Escherichia coli
    • K Jung A Altendorf Towards an understanding of the molecular mechanisms of stimulus perception and signal transduction by the KdpD/KdpE system of Escherichia coli J. Mol. Microbiol. Biotechnol. 4 2002 223 228
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 223-228
    • Jung, K1    Altendorf, A2
  • 115
    • 0035191622 scopus 로고    scopus 로고
    • trans-acting mutations in loci other than kdpDE that affect kdp operon regulation in Escherichia coli: effects of cytoplasmic thiol oxidation status and nucleoid protein H-NS on kdp expression
    • A.A Sardesai J Gowrishankar trans -acting mutations in loci other than kdpDE that affect kdp operon regulation in Escherichia coli : effects of cytoplasmic thiol oxidation status and nucleoid protein H-NS on kdp expression J. Bacteriol. 183 2001 86 93
    • (2001) J. Bacteriol. , vol.183 , pp. 86-93
    • Sardesai, A.A1    Gowrishankar, J2
  • 116
    • 0031686597 scopus 로고    scopus 로고
    • Expression of the Kdp ATPase is consistent with regulation by turgor pressure
    • R Malli W Epstein Expression of the Kdp ATPase is consistent with regulation by turgor pressure J. Bacteriol. 180 1998 5102 5108
    • (1998) J. Bacteriol. , vol.180 , pp. 5102-5108
    • Malli, R1    Epstein, W2
  • 117
    • 0027181944 scopus 로고
    • Regulation of kdp operon expression in Escherichia coli: evidence aganst turgor as a signal for transcriptional control
    • H Asha J Gowrishankar Regulation of kdp operon expression in Escherichia coli : evidence aganst turgor as a signal for transcriptional control J. Bacteriol. 175 1993 4528 4537
    • (1993) J. Bacteriol. , vol.175 , pp. 4528-4537
    • Asha, H1    Gowrishankar, J2
  • 118
    • 0028090288 scopus 로고
    • Signal-sensing mechanisms of the putative osmosensor KdpD in Escherichia coli
    • A Sugiura K Hirokawa K Nakashima T Mizuno Signal-sensing mechanisms of the putative osmosensor KdpD in Escherichia coli Mol. Microbiol. 14 1994 929 938
    • (1994) Mol. Microbiol. , vol.14 , pp. 929-938
    • Sugiura, A1    Hirokawa, K2    Nakashima, K3    Mizuno, T4
  • 119
    • 0036420531 scopus 로고    scopus 로고
    • Amino acid replacements in transmembrane domain 1 influence osmosensing but not K+ sensing by the sensor kinase KdpD of Escherichia coli
    • + sensing by the sensor kinase KdpD of Escherichia coli Arch. Microbiol. 178 2002 525 530
    • (2002) Arch. Microbiol. , vol.178 , pp. 525-530
    • Stallkamp, I1    Altendorf, K2    Jung, K3
  • 120
    • 0022974414 scopus 로고
    • Osmotic regulation of transcription: induction of the proU transport gene is dependent on accumulation of intracellular potassium
    • L Sutherland J Cairney M.J Elmore I.R Booth C.F Higgins Osmotic regulation of transcription: induction of the proU transport gene is dependent on accumulation of intracellular potassium J. Bacteriol. 168 1986 804 814
    • (1986) J. Bacteriol. , vol.168 , pp. 804-814
    • Sutherland, L1    Cairney, J2    Elmore, M.J3    Booth, I.R4    Higgins, C.F5
  • 121
    • 0027454334 scopus 로고
    • Functional reconstitution of the putative Escherichia coli osmosensor, KdpD, into liposomes
    • K Nakashima A Sugiura T Mizuno Functional reconstitution of the putative Escherichia coli osmosensor, KdpD, into liposomes J. Biochem. 114 1993 615 621
    • (1993) J. Biochem. , vol.114 , pp. 615-621
    • Nakashima, K1    Sugiura, A2    Mizuno, T3
  • 122
    • 0034704146 scopus 로고    scopus 로고
    • K+ and ionic strength directly influence the autophosphorylation activity of the putative turgor sensor KdpD of Escherichia coli
    • + and ionic strength directly influence the autophosphorylation activity of the putative turgor sensor KdpD of Escherichia coli J. Biol. Chem. 275 2000 40142 40147
    • (2000) J. Biol. Chem. , vol.275 , pp. 40142-40147
    • Jung, K1    Veen, M2    Altendorf, K3
  • 123
    • 0034537416 scopus 로고    scopus 로고
    • Modulation of KdpD phosphatase implicated in the physiological expression of the Kdp ATPase of Escherichia coli
    • L Brandon S Dorus W Epstein K Altendorf K Jung Modulation of KdpD phosphatase implicated in the physiological expression of the Kdp ATPase of Escherichia coli Mol. Microbiol. 38 2000 1086 1092
    • (2000) Mol. Microbiol. , vol.38 , pp. 1086-1092
    • Brandon, L1    Dorus, S2    Epstein, W3    Altendorf, K4    Jung, K5
  • 124
    • 0027511120 scopus 로고
    • Signal transduction between the two regulatory components involved in the regulation of the kdpABC operon in Escherichia coli: phosphorylation-dependent functioning of the positive regulator, KdpE
    • K Nakashima A Sugiura K Kanamaru T Mizuno Signal transduction between the two regulatory components involved in the regulation of the kdpABC operon in Escherichia coli : phosphorylation-dependent functioning of the positive regulator, KdpE Mol. Microbiol. 7 1993 109 116
    • (1993) Mol. Microbiol. , vol.7 , pp. 109-116
    • Nakashima, K1    Sugiura, A2    Kanamaru, K3    Mizuno, T4
  • 125
    • 0029743420 scopus 로고    scopus 로고
    • Characterization of truncated forms of the KdpD protein, the sensor kinase of the K+-translocating Kdp system of Escherichia coli
    • +-translocating Kdp system of Escherichia coli J. Biol. Chem. 271 1996 25027 25034
    • (1996) J. Biol. Chem. , vol.271 , pp. 25027-25034
    • Puppe, W1    Zimmann, P2    Jung, K3    Lucassen, M4    Altendorf, K5
  • 127
    • 0025437968 scopus 로고
    • Enteric bacteria and osmotic stress: intracellular potassium glutamate as a secondary signal of osmotic stress
    • I.R Booth C.F Higgins Enteric bacteria and osmotic stress: intracellular potassium glutamate as a secondary signal of osmotic stress FEMS Microbiol. Lett. 75 1990 239 246
    • (1990) FEMS Microbiol. Lett. , vol.75 , pp. 239-246
    • Booth, I.R1    Higgins, C.F2
  • 128
    • 0036239754 scopus 로고    scopus 로고
    • Bacterial osmoadaptation: the role of osmolytes in bacterial stress and virulence
    • R.D Sleator C Hill Bacterial osmoadaptation: the role of osmolytes in bacterial stress and virulence FEMS Microbiol. Rev. 26 2001 49 71
    • (2001) FEMS Microbiol. Rev. , vol.26 , pp. 49-71
    • Sleator, R.D1    Hill, C2
  • 129
    • 0001570910 scopus 로고    scopus 로고
    • Osmoregulation
    • L.N Csonka W Epstein Osmoregulation F.C Neidhardt R Curtiss III J.L Ingraham E.C.C Lin K.B Low B Magasanik W.S Reznikoff M Riley M Schaechter H.E Umbarger Escherichia coli and Salmonella typhimurium , Cellular and Molecular Biology I (1996) ASM Press Washington, DC 1210 1223
    • (1996) , pp. 1210-1223
    • Csonka, L.N1    Epstein, W2
  • 130
    • 0031719418 scopus 로고    scopus 로고
    • Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments
    • B Kempf E Bremer Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments Arch. Microbiol. 170 1998 319 330
    • (1998) Arch. Microbiol. , vol.170 , pp. 319-330
    • Kempf, B1    Bremer, E2
  • 133
    • 0036904138 scopus 로고    scopus 로고
    • Body shaping under water stress: osmosensing and osmoregulation of solute transport in bacteria
    • S Morbach R Krämer Body shaping under water stress: osmosensing and osmoregulation of solute transport in bacteria ChemBioChem. 3 2002 384 397
    • (2002) ChemBioChem. , vol.3 , pp. 384-397
    • Morbach, S1    Krämer, R2
  • 134
    • 0032579253 scopus 로고    scopus 로고
    • Osmo-sensing by N- and C-terminal extensions of the glycine betaine uptake system BetP of Corynebacterium glutamicum
    • H Peter A Burkovski R Krämer Osmo-sensing by N- and C-terminal extensions of the glycine betaine uptake system BetP of Corynebacterium glutamicum J. Biol. Chem. 273 1998 2567 2574
    • (1998) J. Biol. Chem. , vol.273 , pp. 2567-2574
    • Peter, H1    Burkovski, A2    Krämer, R3
  • 135
    • 0023755693 scopus 로고
    • Proline porter II is activated by a hyperosmotic shift in both whole cells and membrane vesicles of Escherichia coli
    • J.L Milner S Grothe J.M Wood Proline porter II is activated by a hyperosmotic shift in both whole cells and membrane vesicles of Escherichia coli J. Biol. Chem. 263 1990 14900 14905
    • (1990) J. Biol. Chem. , vol.263 , pp. 14900-14905
    • Milner, J.L1    Grothe, S2    Wood, J.M3
  • 136
    • 0037457916 scopus 로고    scopus 로고
    • Osmosensor ProP of Escherichia coli responds to the concentration, chemistry and molecular size of osmolytes in the proteoliposome lumen
    • D.E Culham J Henderson R.A Crane J.M Wood Osmosensor ProP of Escherichia coli responds to the concentration, chemistry and molecular size of osmolytes in the proteoliposome lumen Biochemistry 42 2003 410 420
    • (2003) Biochemistry , vol.42 , pp. 410-420
    • Culham, D.E1    Henderson, J2    Crane, R.A3    Wood, J.M4
  • 137
    • 0033988625 scopus 로고    scopus 로고
    • Glycine betaine transport in Lactococcus lactis is osmotically regulated at the level of expression and translocation activity
    • T van der Heide B Poolman Glycine betaine transport in Lactococcus lactis is osmotically regulated at the level of expression and translocation activity J. Bacteriol. 182 2000 203 206
    • (2000) J. Bacteriol. , vol.182 , pp. 203-206
    • van der Heide, T1    Poolman, B2
  • 138
    • 0034691129 scopus 로고    scopus 로고
    • Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane
    • T van der Heide B Poolman Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane Proc. Natl. Acad. Sci. USA 97 2000 7102 7106
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7102-7106
    • van der Heide, T1    Poolman, B2
  • 139
    • 0037126588 scopus 로고    scopus 로고
    • On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine
    • T van der Heide M.C.A Stuart B Poolman On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine EMBO J. 20 2001 7022 7032
    • (2001) EMBO J. , vol.20 , pp. 7022-7032
    • van der Heide, T1    Stuart, M.C.A2    Poolman, B3
  • 140
    • 0033601291 scopus 로고    scopus 로고
    • Lipid-assisted protein folding
    • M Bogdanov W Dowhan Lipid-assisted protein folding J. Biol. Chem. 274 1999 36827 36830
    • (1999) J. Biol. Chem. , vol.274 , pp. 36827-36830
    • Bogdanov, M1    Dowhan, W2
  • 141
    • 0027423545 scopus 로고
    • Bacterial solute transport proteins in their lipid environment
    • G.I Veld A.J Driesen W.N Konings Bacterial solute transport proteins in their lipid environment FEMS Microbiol. Rev. 12 1993 293 314
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 293-314
    • Veld, G.I1    Driesen, A.J2    Konings, W.N3
  • 143
    • 0022349278 scopus 로고
    • Regulation of cytoplasmic pH in bacteria
    • I.R Booth Regulation of cytoplasmic pH in bacteria Microbiol. Rev. 49 1985 359 378
    • (1985) Microbiol. Rev. , vol.49 , pp. 359-378
    • Booth, I.R1
  • 144
    • 0032616511 scopus 로고    scopus 로고
    • The regulation of intracellular pH in bacteria
    • I.R Booth The regulation of intracellular pH in bacteria Novartis Found. Symp. 221 1999 19 28
    • (1999) Novartis Found. Symp. , vol.221 , pp. 19-28
    • Booth, I.R1
  • 145
    • 0029884672 scopus 로고    scopus 로고
    • The activity of the high-affinity potassium uptake system Kdp sensitises cells of Escherichia coli to methylglyoxal
    • G.P Ferguson A.D Chacko C Lee I.R Booth The activity of the high-affinity potassium uptake system Kdp sensitises cells of Escherichia coli to methylglyoxal J. Bacteriol. 178 1996 3957 39661
    • (1996) J. Bacteriol. , vol.178 , pp. 3957-39661
    • Ferguson, G.P1    Chacko, A.D2    Lee, C3    Booth, I.R4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.