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Volumn 428, Issue , 2007, Pages 487-504

Methods of Changing Biopolymer Volume Fraction and Cytoplasmic Solute Concentrations for In Vivo Biophysical Studies

Author keywords

[No Author keywords available]

Indexed keywords

BETAINE; BIOPOLYMER; CHOLINE; ECTOINE; GLUTAMIC ACID; GLYCEROL; NUCLEIC ACID; OLIGOSACCHARIDE; POTASSIUM ION; PROLINE; PUTRESCINE; TREHALOSE; UREA;

EID: 35748977127     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)28027-9     Document Type: Chapter
Times cited : (24)

References (49)
  • 1
    • 0034028431 scopus 로고    scopus 로고
    • Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress
    • Cayley D.S., Guttman H.J., and Record Jr. M.T. Biophysical characterization of changes in 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.S.1    Guttman, H.J.2    Record Jr., M.T.3
  • 2
    • 0026409841 scopus 로고
    • Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity: Implications for protein-DNA interactions in vivo
    • Cayley S., Lewis B.A., Guttman H.J., and Record Jr. M.T. Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity: Implications for protein-DNA interactions in vivo. J. Mol. Biol. 222 (1991) 281-300
    • (1991) J. Mol. Biol. , vol.222 , pp. 281-300
    • Cayley, S.1    Lewis, B.A.2    Guttman, H.J.3    Record Jr., M.T.4
  • 3
    • 0026559541 scopus 로고
    • Origins of the osmoprotective properties of betaine and proline in Escherichia coli K-12
    • Cayley S., Lewis B.A., and Record Jr. M.T. Origins of the osmoprotective properties of betaine and proline in Escherichia coli K-12. J. Bacteriol. 174 (1992) 1586-1595
    • (1992) J. Bacteriol. , vol.174 , pp. 1586-1595
    • Cayley, S.1    Lewis, B.A.2    Record Jr., M.T.3
  • 4
    • 0242286667 scopus 로고    scopus 로고
    • Roles of cytoplasmic osmolytes, water, and crowding in the response of Escherichia coli to osmotic stress: Biophysical basis of osmoprotection by glycine betaine
    • Cayley S., and Record Jr. M.T. Roles of cytoplasmic osmolytes, water, and crowding in the response of Escherichia coli to osmotic stress: Biophysical basis of osmoprotection by glycine betaine. Biochemistry 42 (2003) 12596-12609
    • (2003) Biochemistry , vol.42 , pp. 12596-12609
    • Cayley, S.1    Record Jr., M.T.2
  • 5
    • 0024358860 scopus 로고
    • Accumulation of 3-(N-morpholino)propanesulfonate by osmotically stressed Escherichia coli K-12
    • Cayley S., Record Jr. M.T., and Lewis B.A. Accumulation of 3-(N-morpholino)propanesulfonate by osmotically stressed Escherichia coli K-12. J. Bacteriol. 171 (1989) 3597-3602
    • (1989) J. Bacteriol. , vol.171 , pp. 3597-3602
    • Cayley, S.1    Record Jr., M.T.2    Lewis, B.A.3
  • 6
    • 0034009901 scopus 로고    scopus 로고
    • An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells
    • Cluzel P., Surette M., and Leibler S. An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells. Science 287 (2000) 1652-1655
    • (2000) Science , vol.287 , pp. 1652-1655
    • Cluzel, P.1    Surette, M.2    Leibler, S.3
  • 8
    • 0026006215 scopus 로고
    • Prokaryotic osmoregulation: Genetics and physiology
    • Csonka L.N., and Hanson A.D. Prokaryotic osmoregulation: Genetics and physiology. Annu. Rev. Microbiol. 45 (1991) 569-606
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 569-606
    • Csonka, L.N.1    Hanson, A.D.2
  • 9
    • 0023712118 scopus 로고
    • Transient accumulation of potassium glutamate and its replacement by trehalose during adaptation of growing cells of Escherichia coli K-12 to elevated sodium chloride concentrations
    • Dinnbier U., Limpinsel E., Schmid R., and Bakker E.P. Transient accumulation of potassium glutamate and its replacement by trehalose during adaptation of growing cells of Escherichia coli K-12 to elevated sodium chloride concentrations. Arch. Microbiol. 150 (1988) 348-357
    • (1988) Arch. Microbiol. , vol.150 , pp. 348-357
    • Dinnbier, U.1    Limpinsel, E.2    Schmid, R.3    Bakker, E.P.4
  • 10
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis R.J. Macromolecular crowding: Obvious but underappreciated. Trends Biochem. Sci. 26 (2001) 597-604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 12
    • 85005627207 scopus 로고
    • Cation transport in Escherichia coli. V. Regulation of cation content
    • Epstein W., and Schultz S.G. 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, W.1    Schultz, S.G.2
  • 13
    • 8744225646 scopus 로고    scopus 로고
    • The exclusion of glycine betaine from anionic biopolymer surface: Why glycine betaine is an effective osmoprotectant but also a compatible solute
    • Felitsky D.J., Cannon J.G., Capp M.W., Hong J., Van Wynsberghe A.W., Anderson C.F., and Record M.T. The exclusion of glycine betaine from anionic biopolymer surface: Why glycine betaine is an effective osmoprotectant but also a compatible solute. Biochemistry 43 (2004) 14732-14743
    • (2004) Biochemistry , vol.43 , pp. 14732-14743
    • Felitsky, D.J.1    Cannon, J.G.2    Capp, M.W.3    Hong, J.4    Van Wynsberghe, A.W.5    Anderson, C.F.6    Record, M.T.7
  • 14
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • Ghaemmaghami S., and Oas T.G. Quantitative protein stability measurement in vivo. Nat. Struct. Biol. 8 (2001) 879-882
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 15
    • 3843126332 scopus 로고    scopus 로고
    • RNA dynamics in live Escherichia coli cells
    • Golding I., and Cox E.C. RNA dynamics in live Escherichia coli cells. Proc. Natl. Acad. Sci. USA 101 (2004) 11310-11315
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11310-11315
    • Golding, I.1    Cox, E.C.2
  • 16
    • 33644885029 scopus 로고    scopus 로고
    • Physical nature of bacterial cytoplasm
    • Golding I., and Cox E.C. Physical nature of bacterial cytoplasm. Phys. Rev. Lett. 96 (2006) 098102
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 098102
    • Golding, I.1    Cox, E.C.2
  • 17
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin B.A., Adams S.R., and Tsien R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281 (1998) 269-272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 18
    • 0017807816 scopus 로고
    • Concentration dependence of the self-diffusion of human and Lumbricus terrestris hemoglobin
    • Gros G. Concentration dependence of the self-diffusion of human and Lumbricus terrestris hemoglobin. Biophys. J. 22 (1978) 453-468
    • (1978) Biophys. J. , vol.22 , pp. 453-468
    • Gros, G.1
  • 19
    • 0026498015 scopus 로고
    • Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA: Possible thermodynamic origins of the "glutamate effect" on protein-DNA interactions
    • Ha J.H., Capp M.W., Hohenwalter M.D., Baskerville M., and Record Jr. M.T. Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA: Possible thermodynamic origins of the "glutamate effect" on protein-DNA interactions. J. Mol. Biol. 228 (1992) 252-264
    • (1992) J. Mol. Biol. , vol.228 , pp. 252-264
    • Ha, J.H.1    Capp, M.W.2    Hohenwalter, M.D.3    Baskerville, M.4    Record Jr., M.T.5
  • 20
    • 0027293090 scopus 로고
    • Macromolecular diffusion in crowded solutions
    • Han J., and Herzfeld J. Macromolecular diffusion in crowded solutions. Biophys. J. 65 (1993) 1155-1161
    • (1993) Biophys. J. , vol.65 , pp. 1155-1161
    • Han, J.1    Herzfeld, J.2
  • 21
    • 29344437812 scopus 로고    scopus 로고
    • Use of urea and glycine betaine to quantify coupled folding and probe the burial of DNA phosphates in lac repressor-lac operator binding
    • Hong J., Capp M.W., Saecker R.M., and Record Jr. M.T. Use of urea and glycine betaine to quantify coupled folding and probe the burial of DNA phosphates in lac repressor-lac operator binding. Biochemistry 44 (2005) 16896-16911
    • (2005) Biochemistry , vol.44 , pp. 16896-16911
    • Hong, J.1    Capp, M.W.2    Saecker, R.M.3    Record Jr., M.T.4
  • 22
    • 0347004717 scopus 로고    scopus 로고
    • Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
    • Ignatova Z., and Gierasch L.M. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc. Natl. Acad. Sci. USA 101 (2004) 523-528
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 523-528
    • Ignatova, Z.1    Gierasch, L.M.2
  • 23
    • 33748588165 scopus 로고    scopus 로고
    • Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
    • Ignatova Z., and Gierasch L.M. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc. Natl. Acad. Sci. USA 103 (2006) 13357-13361
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13357-13361
    • Ignatova, Z.1    Gierasch, L.M.2
  • 24
    • 0027529545 scopus 로고
    • Determinants of the translational mobility of a small solute in cell cytoplasm
    • Kao H.P., Abney J.R., and Verkman A.S. Determinants of the translational mobility of a small solute in cell cytoplasm. J. Cell Biol. 120 (1993) 175-184
    • (1993) J. Cell Biol. , vol.120 , pp. 175-184
    • Kao, H.P.1    Abney, J.R.2    Verkman, A.S.3
  • 25
    • 0141990272 scopus 로고
    • Osmotic regulation and the biosynthesis of membrane-derived oligosaccharides in Escherichia coli
    • Kennedy E.P. Osmotic regulation and the biosynthesis of membrane-derived oligosaccharides in Escherichia coli. Proc. Natl. Acad. Sci. USA 79 (1982) 1092-1095
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1092-1095
    • Kennedy, E.P.1
  • 27
    • 33144477944 scopus 로고    scopus 로고
    • Solute probes of conformational changes in open complex (RPo) formation by Escherichia coli RNA polymerase at the lambdaPR promoter: Evidence for unmasking of the active site in the isomerization step and for large-scale coupled folding in the subsequent conversion to RPo
    • Kontur W.S., Saecker R.M., Davis C.A., Capp M.W., and Record Jr. M.T. Solute probes of conformational changes in open complex (RPo) formation by Escherichia coli RNA polymerase at the lambdaPR promoter: Evidence for unmasking of the active site in the isomerization step and for large-scale coupled folding in the subsequent conversion to RPo. Biochemistry 45 (2006) 2161-2177
    • (2006) Biochemistry , vol.45 , pp. 2161-2177
    • Kontur, W.S.1    Saecker, R.M.2    Davis, C.A.3    Capp, M.W.4    Record Jr., M.T.5
  • 28
    • 0024448760 scopus 로고
    • Molecular cloning and expression of a locus (mdoA) implicated in the biosynthesis of membrane-derived oligosaccharides in Escherichia coli
    • Lacroix J.M., Tempete M., Menichi B., and Bohin J.P. Molecular cloning and expression of a locus (mdoA) implicated in the biosynthesis of membrane-derived oligosaccharides in Escherichia coli. Mol. Microbiol. 3 (1989) 1173-1182
    • (1989) Mol. Microbiol. , vol.3 , pp. 1173-1182
    • Lacroix, J.M.1    Tempete, M.2    Menichi, B.3    Bohin, J.P.4
  • 29
    • 0022503080 scopus 로고
    • Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli
    • Landfald B., and Strom A.R. Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli. J. Bacteriol. 165 (1986) 849-855
    • (1986) J. Bacteriol. , vol.165 , pp. 849-855
    • Landfald, B.1    Strom, A.R.2
  • 30
    • 0023219316 scopus 로고
    • Replacement of potassium chloride by potassium glutamate dramatically enhances protein-DNA interactions in vitro
    • Leirmo S., Harrison C., Cayley D.S., Burgess R.R., and Record Jr. M.T. Replacement of potassium chloride by potassium glutamate dramatically enhances protein-DNA interactions in vitro. Biochemistry 26 (1987) 2095-2101
    • (1987) Biochemistry , vol.26 , pp. 2095-2101
    • Leirmo, S.1    Harrison, C.2    Cayley, D.S.3    Burgess, R.R.4    Record Jr., M.T.5
  • 31
    • 0033991590 scopus 로고    scopus 로고
    • Cytoarchitecture and physical properties of cytoplasm: Volume, viscosity, diffusion, intracellular surface area
    • Luby-Phelps K. Cytoarchitecture and physical properties of cytoplasm: Volume, viscosity, diffusion, intracellular surface area. Int. Rev. Cytol. 192 (2000) 189-221
    • (2000) Int. Rev. Cytol. , vol.192 , pp. 189-221
    • Luby-Phelps, K.1
  • 32
    • 0028154018 scopus 로고
    • Interdependence of K+ and glutamate accumulation during osmotic adaptation of Escherichia coli
    • McLaggan D., Naprstek J., Buurman E.T., and Epstein W. Interdependence of K+ and glutamate accumulation during osmotic adaptation of Escherichia coli. J. Biol. Chem. 269 (1994) 1911-1917
    • (1994) J. Biol. Chem. , vol.269 , pp. 1911-1917
    • McLaggan, D.1    Naprstek, J.2    Buurman, E.T.3    Epstein, W.4
  • 33
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton A.P. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276 (2001) 10577-10580
    • (2001) J. Biol. Chem. , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 34
    • 25444487734 scopus 로고    scopus 로고
    • Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observations
    • Minton A.P. Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observations. J. Pharm. Sci. 94 (2005) 1668-1675
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1668-1675
    • Minton, A.P.1
  • 35
    • 33646594697 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in three cell environments in Escherichia coli
    • Mullineaux C.W., Nenninger A., Ray N., and Robinson C. Diffusion of green fluorescent protein in three cell environments in Escherichia coli. J. Bacteriol. 188 (2006) 3442-3448
    • (2006) J. Bacteriol. , vol.188 , pp. 3442-3448
    • Mullineaux, C.W.1    Nenninger, A.2    Ray, N.3    Robinson, C.4
  • 36
    • 0015522503 scopus 로고
    • Dependence of the putrescine content of Escherichia coli on the osmotic strength of the medium
    • Munro G.F., Hercules K., Morgan J., and Sauerbier W. Dependence of the putrescine content of Escherichia coli on the osmotic strength of the medium. J. Biol. Chem. 247 (1972) 1272-1280
    • (1972) J. Biol. Chem. , vol.247 , pp. 1272-1280
    • Munro, G.F.1    Hercules, K.2    Morgan, J.3    Sauerbier, W.4
  • 37
    • 0024006767 scopus 로고
    • Tracer diffusion of globular proteins in concentrated protein solutions
    • Muramatsu N., and Minton A.P. Tracer diffusion of globular proteins in concentrated protein solutions. Proc. Natl. Acad. Sci. USA 85 (1988) 2984-2988
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2984-2988
    • Muramatsu, N.1    Minton, A.P.2
  • 39
    • 4544384311 scopus 로고    scopus 로고
    • Studies of effects of macromolecular crowding and confinement on protein folding and protein stability
    • Ping G., Yuan J.M., Sun Z., and Wei Y. Studies of effects of macromolecular crowding and confinement on protein folding and protein stability. J. Mol. Recogn. 17 (2004) 433-440
    • (2004) J. Mol. Recogn. , vol.17 , pp. 433-440
    • Ping, G.1    Yuan, J.M.2    Sun, Z.3    Wei, Y.4
  • 40
    • 0344653612 scopus 로고    scopus 로고
    • Responses of E. coli to osmotic stress: Large changes in amounts of cytoplasmic solutes and water
    • Record Jr. M.T., Courtenay E.S., Cayley D.S., and Guttman H.J. Responses of E. coli to osmotic stress: Large changes in amounts of cytoplasmic solutes and water. Trends Biochem. Sci. 23 (1998) 143-148
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 143-148
    • Record Jr., M.T.1    Courtenay, E.S.2    Cayley, D.S.3    Guttman, H.J.4
  • 41
    • 0023664450 scopus 로고
    • Variability of the intracellular ionic environment of Escherichia coli: Differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene expression
    • Richey B., Cayley D.S., Mossing M.C., Kolka C., Anderson C.F., Farrar T.C., and Record Jr. M.T. Variability of the intracellular ionic environment of Escherichia coli: Differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene expression. J. Biol. Chem. 262 (1987) 7157-7164
    • (1987) J. Biol. Chem. , vol.262 , pp. 7157-7164
    • Richey, B.1    Cayley, D.S.2    Mossing, M.C.3    Kolka, C.4    Anderson, C.F.5    Farrar, T.C.6    Record Jr., M.T.7
  • 42
    • 0029558909 scopus 로고
    • Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy
    • Terry B.R., Matthews E.K., and Haseloff J. Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy. Biochem. Biophys. Res. Commun. 217 (1995) 21-27
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 21-27
    • Terry, B.R.1    Matthews, E.K.2    Haseloff, J.3
  • 44
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by bacteria: Signals and membrane-based sensors
    • Wood J.M. Osmosensing by bacteria: Signals and membrane-based sensors. Microbiol. Mol. Biol. Rev. 63 (1999) 230-262
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 230-262
    • Wood, J.M.1
  • 45
  • 46
    • 0000225096 scopus 로고
    • Macromolecular crowding increases binding of DNA polymerase to DNA: An adaptive effect
    • Zimmerman S.B., and Harrison B. Macromolecular crowding increases binding of DNA polymerase to DNA: An adaptive effect. Proc. Natl. Acad. Sci. USA 84 (1987) 1871-1875
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1871-1875
    • Zimmerman, S.B.1    Harrison, B.2
  • 47
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman S.B., and Minton A.P. Macromolecular crowding: Biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22 (1993) 27-65
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 48
    • 0023902229 scopus 로고
    • Macromolecular crowding extends the range of conditions under which DNA polymerase is functional
    • Zimmerman S.B., and Trach S.O. Macromolecular crowding extends the range of conditions under which DNA polymerase is functional. Biochim. Biophys. Acta 949 (1988) 297-304
    • (1988) Biochim. Biophys. Acta , vol.949 , pp. 297-304
    • Zimmerman, S.B.1    Trach, S.O.2
  • 49
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • Zimmerman S.B., and Trach S.O. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J. Mol. Biol. 222 (1991) 599-620
    • (1991) J. Mol. Biol. , vol.222 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2


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