Startseite Protein aggregation in crowded environments
Artikel
Lizenziert
Nicht lizenziert Erfordert eine Authentifizierung

Protein aggregation in crowded environments

  • R. John Ellis und Allen P. Minton
Veröffentlicht/Copyright: 1. Juni 2006
Biological Chemistry
Aus der Zeitschrift Band 387 Heft 5

Abstract

The generic tendency of proteins to aggregate into non-functional, and sometimes cytotoxic, structures poses a universal problem for all types of cell. This tendency is greatly exacerbated by the high total concentration of macromolecules found within most intracellular compartments, a phenomenon referred to as macromolecular crowding. This review discusses the quantitative effects of crowding on protein aggregation and the role of molecular chaperones in combating this problem.

:

Corresponding author

References

Acampora, G. and Hermans, J. Jr. (1966). Reversible denaturation of sperm whale myoglobin I. Dependence on temperature, pH and composition. J. Am. Chem. Soc.89, 1543–1547.Suche in Google Scholar

Anfinsen, C.B. (1973). Principles that govern the folding of protein chains. Science181, 231–230.10.1126/science.181.4096.223Suche in Google Scholar

Atha, D.H. and Ingham, K.C. (1981). Mechanism of precipitation of proteins by polyethylene glycol. Analysis in terms of excluded volume. J. Biol. Chem.256, 12108–12117.Suche in Google Scholar

Betancourt, M.R. and Thirumalai, D. (1999). Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity. J. Mol. Biol.287, 627–644.10.1006/jmbi.1999.2591Suche in Google Scholar

Betts, S., Haase-Pettingell, C., and King, J. (1997). Mutational effects on inclusion body formation. Adv. Protein Chem.50, 243–264.10.1016/S0065-3233(08)60323-XSuche in Google Scholar

Boublík, T. (1974). Statistical thermodynamics of convex molecule fluids. Mol. Phys.27, 1415–1427.10.1080/00268977400101191Suche in Google Scholar

Brinker, A., Pfeifer, G., Kerner, M.J., Naylor, D.J., Hartl, F.U., and Hayer-Hartl, M. (2001). Dual function of protein confinement in chaperonin-assisted protein folding. Cell107, 223–233.10.1016/S0092-8674(01)00517-7Suche in Google Scholar

Chargé, S.B.P., de Koning, E.J.P., and Clark, A. (1995). Effects of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro. Biochemistry34, 14588–14593.10.1021/bi00044a038Suche in Google Scholar

Cotter, M.A. (1977). Hard spherocylinder in an anisotropic mean field: a simple model for a nematic liquid crystal. J. Chem. Phys.66, 1098–1106.10.1063/1.434044Suche in Google Scholar

Crick, F.H.C. (1958). On protein synthesis. Symp. Soc. Exp. Biol.13, 138–163.Suche in Google Scholar

Cuneo, P., Magri, E., Verzola, A., and Grazi, E. (1992). ‘Macromolecular crowding’ is a primary factor in the organization of the cytoskeleton. Biochem. J.281, 507–512.10.1042/bj2810507Suche in Google Scholar

Dinner, A.R., Sali, A., Smith, L.J., Dobson, C.M., and Karplus, M. (2000). Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem. Sci.25, 331–339.10.1016/S0968-0004(00)01610-8Suche in Google Scholar

Dobson, C.M. (2001). The structural basis for protein folding and its links with human disease. Phil. Trans. R. Soc. B356, 133–145.10.1098/rstb.2000.0758Suche in Google Scholar PubMed PubMed Central

Dobson, C.M., Ellis, R.J., and Fersht, A.R. (2001). Protein misfolding and disease. Phil. Trans. R. Soc. B356, 127–227.Suche in Google Scholar

Drenckhahn, D. and Pollard, T.D. (1986). Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J. Biol. Chem.261, 12754–12758.10.1016/S0021-9258(18)67157-1Suche in Google Scholar

Eaton, W.A. and Hofrichter, J. (1990). Sickle cell hemoglobin polymerization. Adv. Protein Chem.40, 63–279.10.1016/S0065-3233(08)60287-9Suche in Google Scholar

Ellis, R.J. (2001). Macromolecular crowding: obvious but under-appreciated. Trends Biochem. Sci.26, 597–604.10.1016/S0968-0004(01)01938-7Suche in Google Scholar

Ellis, R.J. (2003). Protein folding: importance of the Anfinsen cage. Curr. Biol.13, R881–R883.10.1016/j.cub.2003.10.051Suche in Google Scholar

Ellis, R.J. and Hemmingsen, S.M. (1989). Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci.14, 339–342.10.1016/0968-0004(89)90168-0Suche in Google Scholar

Epstein, C.J., Goldberger, R.F., and Anfinsen, C.B. (1963). The genetic control of tertiary protein structure: studies with model systems. Cold Spring Harbor Symp. Quant. Biol.28, 439–449.10.1101/SQB.1963.028.01.060Suche in Google Scholar

Ferrone, F.A. and Rotter, M.A. (2004). Crowding and the polymerization of sickle hemoglobin. J. Mol. Recognit.17, 497–504.10.1002/jmr.698Suche in Google Scholar

Fulton, A.B. (1982). How crowded is the cytoplasm? Cell30, 345–347.10.1016/0092-8674(82)90231-8Suche in Google Scholar

Giddings, J.C., Kucera, E., Russell, C.P., and Myers, N.M. (1968). Statistical theory for the equilibrium distribution of rigid molecules in inert porous networks. Exclusion chromatography. J. Phys. Chem.72, 4397–4408.Suche in Google Scholar

Goldberg, M.E., Rudolph, R., and Jaenicke, R. (1991). A kinetic study of the competition between renaturation and aggregation during refolding of denatured reduced egg white lysozyme. Biochemistry30, 2790–2797.10.1021/bi00225a008Suche in Google Scholar PubMed

Gonzalez, J., Jimenez, M., Velez, M., Mingorance, J., Andreu, J.M., Vicente, M., and Rivas, G. (2003). Essential cell division protein FtsZ assembles into one-monomer-thick ribbons under conditions resembling the crowded intracellular environment. J. Biol. Chem.278, 37664–37671.10.1074/jbc.M305230200Suche in Google Scholar PubMed

Hall, D. and Minton, A.P. (2002). Effects of inert volume-excluding macromolecules on protein fiber formation. I. Equilibrium models. Biophys. Chem.98, 93–104.Suche in Google Scholar

Hall, D. and Minton, A.P. (2004). Effects of inert volume-excluding macromolecules on protein fiber formation.II. Kinetic models for nucleated fiber growth. Biophys. Chem.107, 299–316.Suche in Google Scholar

Hartl, F.U. and Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science295, 1852–1858.10.1126/science.1068408Suche in Google Scholar

Hatters, D.M., Minton, A.P., and Howlett, G.J. (2002). Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II. J. Biol. Chem.277, 7824–7830.10.1074/jbc.M110429200Suche in Google Scholar

Jaenicke, R. and Seckler, R. (1997). Protein misassembly in vitro. Adv. Protein Chem.50, 1–53.10.1016/S0065-3233(08)60318-6Suche in Google Scholar

Kiseleva, E.V. (1989). Secretory protein synthesis in Chironomus salivary gland cells is not coupled with protein translocation across endoplasmic reticulum membranes. FEBS Lett.257, 251–253.10.1016/0014-5793(89)81545-5Suche in Google Scholar

Kocisko, D.A., Priola, S.A., Raymond, D.J., Chesbro, B., Lansbury, P.T., and Caughey, B. (1995). Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. Proc. Natl. Acad. Sci. USA92, 3923–3927.10.1073/pnas.92.9.3923Suche in Google Scholar

Laurent, T.C. (1963). The interaction between polysaccharides and other macromolecules. The solubility of proteins in the presence of dextran. Biochem. J.89, 253–257.Suche in Google Scholar

Lazaridis, T. and Karplus, M. (1997). ‘New view’ of protein folding reconciled with the old through multiple unfolding simulations. Science278, 1928–1931.10.1126/science.278.5345.1928Suche in Google Scholar

Lebowitz, J.L., Helfand, E., and Praestgaard, E. (1965). Scaled particle theory of fluid mixtures. J. Chem. Phys.43, 774–779.10.1063/1.1696842Suche in Google Scholar

Li, J., Zhang, S., and Wang, C.-C. (2001) Effects of macromolecular crowding on the refolding of glucose-6-phosphate dehydrogenase and protein disulfide isomerase. J. Biol. Chem.276, 34396–34401.10.1074/jbc.M103392200Suche in Google Scholar

Lindner, R.A. and Ralston, G.B. (1997). Macromolecular crowding: effects on actin polymerization. Biophys. Chem.66, 57–66.10.1016/S0301-4622(97)00011-2Suche in Google Scholar

London, J., Skrzynia, C., and Goldberg, M. (1974). Renaturation of Escherichia coli tryptophanase in aqueous urea solutions. Eur. J. Biochem.47, 409–415.10.1111/j.1432-1033.1974.tb03707.xSuche in Google Scholar PubMed

Martin, J. (2002). Requirement for GroEL/GroES-dependent protein folding under non-permissive conditions of macromolecular crowding. Biochemistry41, 5050–5055.10.1021/bi015925lSuche in Google Scholar

Martin, J. (2004). Chaperonin function – effects of crowding and confinement. J. Mol. Recognit.17, 465–472.10.1002/jmr.707Suche in Google Scholar

Martin, J. and Hartl, F.U. (1997). The effect of macromolecular crowding on chaperonin-mediated protein folding. Proc. Natl. Acad. Sci. USA94, 1107–1112.10.1073/pnas.94.4.1107Suche in Google Scholar

Minton, A.P. (1981). Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers20, 2093–2120.10.1002/bip.1981.360201006Suche in Google Scholar

Minton, A.P. (1983). The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences. Mol. Cell. Biochem.55, 119–140.10.1007/BF00673707Suche in Google Scholar

Minton, A.P. (1992). Confinement as a determinant of macromolecular structure. Biophys. J.63, 1090–1100.10.1016/S0006-3495(92)81663-6Suche in Google Scholar

Minton, A.P. (1998). Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion. Methods Enzymol.295127–149.10.1016/S0076-6879(98)95038-8Suche in Google Scholar

Minton, A.P. (2000). Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol.10, 34–39.10.1016/S0959-440X(99)00045-7Suche in Google Scholar

Minton, A.P. (2001a). The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem.276, 10577–10580.10.1074/jbc.R100005200Suche in Google Scholar

Minton, A.P. (2001b). Effects of excluded surface area and adsorbate clustering on surface adsorption of proteins. II. Kinetic models. Biophys. J.80, 1641–1648.10.1016/S0006-3495(01)76136-XSuche in Google Scholar

Minton, K.W., Karmin, P., Hahn, G.M., and Minton, A.P. (1982). Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins. Proc. Natl. Acad. Sci. USA79, 7107–7111.10.1073/pnas.79.23.7107Suche in Google Scholar

Ogston, A.G. (1958). The spaces in a uniform random suspension of fibres. Trans. Faraday Soc.5, 1754–1757.10.1039/tf9585401754Suche in Google Scholar

Rivas, G., Fernandez, J.A., and Minton, A.P. (1999). Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance. Biochemistry38, 9379–9388.10.1021/bi990355zSuche in Google Scholar

Rivas, G., Fernandez, J.A., and Minton, A.P. (2001). Direct observation of the enhancement of non-cooperative protein self-assembly by macromolecular crowding: indefinite linear self-association of bacterial cell division protein FtsZ. Proc. Natl. Acad. Sci. USA98, 3150–3155.10.1073/pnas.051634398Suche in Google Scholar

Ross, P.D. and Minton, A.P. (1977). Analysis of nonideal behavior in concentrated hemoglobin solutions. J. Mol. Biol.112, 437–452.10.1016/S0022-2836(77)80191-5Suche in Google Scholar

Ross, P.D. and Minton, A.P. (1979). The effect of non-aggregating proteins upon the gelation of sickle cell hemoglobin: model calculations and data analysis. Biochem. Biophys. Res. Commun.88, 1308–1314.10.1016/0006-291X(79)91123-9Suche in Google Scholar

Sasahara, K., McPhie, P., and Minton, A.P. (2004). Effect of dextran on protein stability and conformation attributed to macromolecular crowding. J. Mol. Biol.326, 1227–1237.Suche in Google Scholar

Shtilerman, M.D., Ding, T.T., and Lansbury, P.T. (2002). Molecular crowding accelerates fibrillization of α-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry41, 3855–3860.10.1021/bi0120906Suche in Google Scholar

Soti, C. and Csermely, P. (2000). Molecular chaperones and the aging process. Biogerentology1, 225–233.10.1023/A:1010082129022Suche in Google Scholar

Speed, M.A., Wang, D.I.C., and King, J. (1996). Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nat. Biotechnol.14, 1283–1287.10.1038/nbt1096-1283Suche in Google Scholar

Sunde, M. and Blake, C. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem.50, 123–160.10.1016/S0065-3233(08)60320-4Suche in Google Scholar

Takagi, F., Koga, N., and Takada, S. (2003). How protein thermodynamics and folding are altered by the chaperonin cage: molecular simulations. Proc. Natl. Acad. Sci. USA100, 11367–11372.10.1073/pnas.1831920100Suche in Google Scholar

Tokuriki, N., Kinjo, M., Negi, S., Hoshino, M., Goto, Y., Urabe, I., and Yomo, T. (2004). Protein folding by the effects of macromolecular crowding. Protein Sci.13, 125–133.10.1110/ps.03288104Suche in Google Scholar

Uversky, V.N., Cooper, E.M., Bower, J.I., and Fink, A.L. (2002). Accelerated α-synuclein fibrillation in crowded mileu. FEBS Lett.515, 99–103.10.1016/S0014-5793(02)02446-8Suche in Google Scholar

Van den Berg, B., Ellis, R.J., and Dobson, C.M. (1999). Effects of macromolecular crowding on protein folding and aggregation. EMBO J.18, 6927–6933.10.1093/emboj/18.24.6927Suche in Google Scholar

Van den Berg, B., Wain, R., Dobson, C.M., and Ellis, R.J. (2000). Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J.19, 3870–3875.10.1093/emboj/19.15.3870Suche in Google Scholar

Walsh, D.M., Klyubin, I., Fadeeva, J.V., Cullen, W.K., Anwyl, R., Wolfe, M.S., Rowan, M.J., and Selkoe, D.J. (2002). Naturally secreted oligomers of amyloid-protein potently inhibit hippocampal long-term potentiation in vivo. Nature416, 535–539.10.1038/416535aSuche in Google Scholar

Wenner, J.R. and Bloomfield, V.A. (1999). Crowding effects on EcoRV kinetics and binding. Biophys. J.77, 3234–3241.10.1016/S0006-3495(99)77154-7Suche in Google Scholar

Wilf, J., Gladner, J.A., and Minton, A.P. (1985). Acceleration of fibrin gel formation by unrelated proteins. Thromb. Res.37, 681–688.10.1016/0049-3848(85)90197-5Suche in Google Scholar

Zettmeissl, G., Rudolph, R., and Jaenicke, R. (1979). Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. Biochemistry18, 5567–5571.Suche in Google Scholar

Zhou, H.-X. and Dill, K.A. (2001). Stabilization of proteins in confined spaces. Biochemistry40, 1289–1293.10.1021/bi0155504Suche in Google Scholar PubMed

Zimmerman, S.B. and Minton, A.P. (1993). Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct.22, 27–65.10.1146/annurev.bb.22.060193.000331Suche in Google Scholar PubMed

Zimmerman, S.B. and Trach, S.O. (1991). Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of E. coli. J. Mol. Biol.222, 599–620.10.1016/0022-2836(91)90499-VSuche in Google Scholar

Published Online: 2006-06-01
Published in Print: 2006-05-01

©2006 by Walter de Gruyter Berlin New York

Artikel in diesem Heft

  1. Protein aggregation in crowded environments
  2. Nitrite, a naturally occurring precursor of nitric oxide that acts like a ‘prodrug’
  3. Functional studies of the small subunit of EcoHK31I DNA methyltransferase
  4. Functional analysis of amino acid residues at the dimerisation interface of KpnI DNA methyltransferase
  5. Conformation and stability of the Streptococcus pyogenes pSM19035-encoded site-specific β recombinase, and identification of a folding intermediate
  6. Tyr-48, a conserved residue in ribotoxins, is involved in the RNA-degrading activity of α-sarcin
  7. Pathogenicity of catalytic antibodies: catalytic activity of Bence Jones proteins from myeloma patients with renal impairment can elicit cytotoxic effects
  8. Transgenic expression of gallerimycin, a novel antifungal insect defensin from the greater wax moth Galleria mellonella, confers resistance to pathogenic fungi in tobacco
  9. Catalytic pathways of Euphorbia characias peroxidase reacting with hydrogen peroxide
  10. Biochemical and pharmacological characterization of the human bradykinin subtype 2 receptor produced in mammalian cells using the Semliki Forest virus system
  11. A spectroscopic analysis of the interaction between the human regulatory proteins RACK1 and Ki-1/57
  12. Subcellular localisation of human inositol 1,4,5-trisphosphate 3-kinase C: species-specific use of alternative export sites for nucleo-cytoplasmic shuttling indicates divergent roles of the catalytic and N-terminal domains
  13. The gating effect of calmodulin and calcium on the connexin50 hemichannel
  14. C-Terminal fusion of eGFP to the bradykinin B2 receptor strongly affects down-regulation but not receptor internalization or signaling
  15. Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII
  16. μ-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation
  17. Cathepsin L splice variants in human breast cell lines
Heruntergeladen am 25.10.2025 von https://www.degruyterbrill.com/document/doi/10.1515/BC.2006.064/html
Button zum nach oben scrollen