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Volumn 188, Issue 17, 2006, Pages 6115-6123

Crowding and confinement effects on protein diffusion in vivo

Author keywords

[No Author keywords available]

Indexed keywords

BIOPOLYMER; GREEN FLUORESCENT PROTEIN; POTASSIUM ION;

EID: 33749018832     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01982-05     Document Type: Article
Times cited : (172)

References (39)
  • 1
    • 0032204171 scopus 로고    scopus 로고
    • Solute diffusion within hydrogels. Mechanisms and models
    • Amsden, B. 1998. Solute diffusion within hydrogels. Mechanisms and models. Macromolecules 31:8382-8395.
    • (1998) Macromolecules , vol.31 , pp. 8382-8395
    • Amsden, B.1
  • 2
    • 27744475701 scopus 로고    scopus 로고
    • Anomalous diffusion of proteins due to molecular crowding
    • Banks, D. S., and C. Fradin. 2005. Anomalous diffusion of proteins due to molecular crowding. Biophys. J. 89:2960-2971.
    • (2005) Biophys. J. , vol.89 , pp. 2960-2971
    • Banks, D.S.1    Fradin, C.2
  • 3
    • 0000640710 scopus 로고    scopus 로고
    • Modulation of the chemical composition and other parameters of the cell by growth rate
    • 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, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Bremer, H., and P. P. Dennis. 1996. Modulation of the chemical composition and other parameters of the cell by growth rate, p. 1553-1569. In 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, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, vol. 2. ASM Press, Washington, D.C.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , vol.2 , pp. 1553-1569
    • Bremer, H.1    Dennis, P.P.2
  • 4
    • 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., H. J. Guttman, and M. T. Record, Jr. 2000. 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. 78:1748-1764.
    • (2000) Biophys. J. , vol.78 , pp. 1748-1764
    • Cayley, D.S.1    Guttman, H.J.2    Record Jr., M.T.3
  • 5
    • 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 M. T. Record, Jr. 2003. Roles of cytoplasmic osmolytes, water, and crowding in the response of Escherichia coli to osmotic stress: biophysical basis of osmoprotection by glycine betaine. Biochemistry 42:12596-12609.
    • (2003) Biochemistry , vol.42 , pp. 12596-12609
    • Cayley, S.1    Record Jr., M.T.2
  • 7
    • 18144393456 scopus 로고    scopus 로고
    • Restricted diffusion of DNA segments within the isolated Escherichia coli nucleoid
    • Cunha, S., C. L. Woldringh, and T. Odijk. 2005. Restricted diffusion of DNA segments within the isolated Escherichia coli nucleoid. J. Struct. Biol. 150:226-232.
    • (2005) J. Struct. Biol. , vol.150 , pp. 226-232
    • Cunha, S.1    Woldringh, C.L.2    Odijk, T.3
  • 8
    • 4544381399 scopus 로고    scopus 로고
    • Molecular crowding reduces to a similar extent the diffusion of small solutes and macromolecules: Measurement by fluorescence correlation spectroscopy
    • Dauty, E., and A. S. Verkman. 2004. Molecular crowding reduces to a similar extent the diffusion of small solutes and macromolecules: measurement by fluorescence correlation spectroscopy. J. Mol. Recognit. 17:441-447.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 441-447
    • Dauty, E.1    Verkman, A.S.2
  • 9
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis, R. J. 2001. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26:597-604.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 11
    • 0028360796 scopus 로고
    • Macromolecular crowding and confinement in cells exposed to hypertonicity
    • Garner, M. M., and M. B. Burg. 1994. Macromolecular crowding and confinement in cells exposed to hypertonicity. Am. J. Physiol. 266:C877-C892.
    • (1994) Am. J. Physiol. , vol.266
    • Garner, M.M.1    Burg, M.B.2
  • 13
    • 14844304655 scopus 로고    scopus 로고
    • The new bacterial cell biology: Moving parts and subcellular architecture
    • Gitai, Z. 2005. The new bacterial cell biology: moving parts and subcellular architecture. Cell 120:577-586.
    • (2005) Cell , vol.120 , pp. 577-586
    • Gitai, Z.1
  • 14
    • 0027293090 scopus 로고
    • Macromolecular diffusion in crowded solutions
    • Han, J., and J. Herzfeld. 1993. Macromolecular diffusion in crowded solutions. Biophys. J. 65:1155-1161.
    • (1993) Biophys. J. , vol.65 , pp. 1155-1161
    • Han, J.1    Herzfeld, J.2
  • 15
    • 0037040878 scopus 로고    scopus 로고
    • Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II
    • Hatters, D. M., A. P. Minton, and G. J. Howlett. 2002. Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II. J. Biol. Chem. 277:7824-7830.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7824-7830
    • Hatters, D.M.1    Minton, A.P.2    Howlett, G.J.3
  • 16
    • 4544297320 scopus 로고    scopus 로고
    • Crowding-induced organization in cells: Spontaneous alignment and sorting of filaments with physiological control points
    • Herzfeld, J. 2004. Crowding-induced organization in cells: spontaneous alignment and sorting of filaments with physiological control points. J. Mol. Recognit. 17:376-381.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 376-381
    • Herzfeld, J.1
  • 17
    • 0036512564 scopus 로고    scopus 로고
    • Dynamic localization of proteins and DNA during a bacterial cell cycle
    • Jensen, R. B., S. C. Wang, and L. Shapiro. 2002. Dynamic localization of proteins and DNA during a bacterial cell cycle. Nat. Rev. Mol. Cell Biol. 3:167-176.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 167-176
    • Jensen, R.B.1    Wang, S.C.2    Shapiro, L.3
  • 18
    • 0027529545 scopus 로고
    • Determinants of the translational mobility of a small solute in cell cytoplasm
    • Kao, H. P., J. R. Abney, and A. S. Verkman. 1993. Determinants of the translational mobility of a small solute in cell cytoplasm. J. Cell Biol. 120:175-184.
    • (1993) J. Cell Biol. , vol.120 , pp. 175-184
    • Kao, H.P.1    Abney, J.R.2    Verkman, A.S.3
  • 19
    • 85010292860 scopus 로고    scopus 로고
    • The biophysics of the gram-negative periplasmic space
    • Koch, A. L. 1998. The biophysics of the gram-negative periplasmic space. Crit. Rev. Microbiol. 24:23-59.
    • (1998) Crit. Rev. Microbiol. , vol.24 , pp. 23-59
    • Koch, A.L.1
  • 20
    • 0028787059 scopus 로고
    • Crowding-induced organization of cytoskeletal elements. III. Spontaneous bundling and sorting of self-assembled filaments with different flexibilities
    • Kulp, D. T., and J. Herzfeld. 1995. Crowding-induced organization of cytoskeletal elements. III. Spontaneous bundling and sorting of self-assembled filaments with different flexibilities. Biophys. Chem. 57:93-102.
    • (1995) Biophys. Chem. , vol.57 , pp. 93-102
    • Kulp, D.T.1    Herzfeld, J.2
  • 22
    • 0026621146 scopus 로고
    • Interactions of Escherichia coli membrane lipoproteins with the murine sacculus
    • Leduc, M., K. Ishidate, N. Shakibai, and L. Rothfield. 1992. Interactions of Escherichia coli membrane lipoproteins with the murine sacculus. J. Bacteriol. 174:7982-7988.
    • (1992) J. Bacteriol. , vol.174 , pp. 7982-7988
    • Leduc, M.1    Ishidate, K.2    Shakibai, N.3    Rothfield, L.4
  • 23
    • 0026730739 scopus 로고
    • Confinement as a determinant of macromolecular structure and reactivity
    • Minton, A. P. 1992. Confinement as a determinant of macromolecular structure and reactivity. Biophys. J. 63:1090-1100.
    • (1992) Biophys. J. , vol.63 , pp. 1090-1100
    • Minton, A.P.1
  • 24
    • 25444487734 scopus 로고    scopus 로고
    • Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observations
    • Minton, A. P. 2005. Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations. J. Pharm. Sci. 94:1668-1675.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1668-1675
    • Minton, A.P.1
  • 25
    • 0019883893 scopus 로고
    • Effect of macromolecular crowding upon the structure and function of an enzyme: Glyceraldehyde-3-phosphate dehydrogenase
    • Minton, A. P., and J. Wilf. 1981. Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 20:4821-4826.
    • (1981) Biochemistry , vol.20 , pp. 4821-4826
    • Minton, A.P.1    Wilf, J.2
  • 26
    • 0024006767 scopus 로고
    • Tracer diffusion of globular proteins in concentrated protein solutions
    • Muramatsu, N., and A. P. Minton. 1988. Tracer diffusion of globular proteins in concentrated protein solutions. Proc. Natl. Acad. Sci. USA 85:2984-2988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2984-2988
    • Muramatsu, N.1    Minton, A.P.2
  • 27
    • 0027943344 scopus 로고
    • Macromolecular crowding effects on the interaction of DNA with Escherichia coli DNA-binding proteins: A model for bacterial nucleoid stabilization
    • Murphy, L. D., and S. B. Zimmerman. 1994. Macromolecular crowding effects on the interaction of DNA with Escherichia coli DNA-binding proteins: a model for bacterial nucleoid stabilization. Biochim. Biophys. Acta 1219:277-284.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 277-284
    • Murphy, L.D.1    Zimmerman, S.B.2
  • 28
    • 0003796783 scopus 로고    scopus 로고
    • Neidhardt, F. C., R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznifcoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). ASM Press, Washington, D.C.
    • Neidhardt, F. C., R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznifcoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). 1996. Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd Ed.
  • 29
    • 0032514107 scopus 로고    scopus 로고
    • Osmotic compaction of supercoiled DNA into a bacterial nucleoid
    • Odijk, T. 1998. Osmotic compaction of supercoiled DNA into a bacterial nucleoid. Biophys. Chem. 73:23-29.
    • (1998) Biophys. Chem. , vol.73 , pp. 23-29
    • Odijk, T.1
  • 30
    • 0008566674 scopus 로고    scopus 로고
    • Structure and dynamics of green fluorescent protein
    • Phillips, G. N., Jr. 1997. Structure and dynamics of green fluorescent protein. Curr. Opin. Struct. Biol. 7:821-827.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 821-827
    • Phillips Jr., G.N.1
  • 32
    • 0027205049 scopus 로고
    • Development and behavior in bacteria
    • Shapiro, L., D. Kaiser, and R. Losick. 1993. Development and behavior in bacteria. Cell 73:835-836.
    • (1993) Cell , vol.73 , pp. 835-836
    • Shapiro, L.1    Kaiser, D.2    Losick, R.3
  • 33
    • 0031000601 scopus 로고    scopus 로고
    • Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion
    • Swaminathan, R., C. P. Hoang, and A. S. Verkman. 1997. Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion. Biophys. J. 72:1900-1907.
    • (1997) Biophys. J. , vol.72 , pp. 1900-1907
    • Swaminathan, R.1    Hoang, C.P.2    Verkman, A.S.3
  • 34
    • 0029558909 scopus 로고
    • Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy
    • Terry, B. R., E. K. Matthews, and J. Haseloff. 1995. Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy. Biochem. Biophys. Res. Commun. 217:21-27.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 21-27
    • Terry, B.R.1    Matthews, E.K.2    Haseloff, J.3
  • 37
    • 0036164351 scopus 로고    scopus 로고
    • Solute and macromolecule diffusion in cellular aqueous compartments
    • Verkman, A. S. 2002. Solute and macromolecule diffusion in cellular aqueous compartments. Trends Biochem. Sci. 27:27-33.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 27-33
    • Verkman, A.S.1
  • 38
    • 0036050398 scopus 로고    scopus 로고
    • The role of cotranscriptional translation and protein translocation (transertion) in bacterial chromosome segregation
    • Woldringh, C. L. 2002. The role of cotranscriptional translation and protein translocation (transertion) in bacterial chromosome segregation. Mol. Microbiol. 45:17-29.
    • (2002) Mol. Microbiol. , vol.45 , pp. 17-29
    • Woldringh, C.L.1
  • 39
    • 0028051862 scopus 로고
    • Significance of plasmolysis spaces as markers for periseptal annuli and adhesion sites
    • Woldringh, C. L. 1994. Significance of plasmolysis spaces as markers for periseptal annuli and adhesion sites. Mol. Microbiol. 14:597-607.
    • (1994) Mol. Microbiol. , vol.14 , pp. 597-607
    • Woldringh, C.L.1


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