Influence of excluded volume upon macromolecular structure and associations in 'crowded' media

Current Opinion in Biotechnology

Volumn 8, Issue 1, 1997, Pages 65-69

  Minton, Allen P ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOPOLYMER;

APTITUDE; CHEMICAL STRUCTURE; CULTURE MEDIUM; MACROMOLECULE; MODEL; PRIORITY JOURNAL; REVIEW; THEORETICAL STUDY; VOLUMETRY;

EID: 0031022118     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(97)80159-0     Document Type: Article

References (44)

1. 1. Fulton AB: How crowded is the cytoplasm? Cell 1982, 30:345-347.
2. 2. Zimmerman SB, Trach SO: Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of E. coli. J Mol Biol 1991, 222:599-620.
3. 3. Timasheff SN: Preferential interactions of water and cosolvents with proteins. In Protein-Solvent Interactions. Edited by Gregory RB. New York: Marcel Dekker; 1995:445-482.
4. 4. Ralston GB: Effects of "crowding" in protein solutions. J Chem Educ 1990, 67:857-860.
5. 5. Zimmerman SB, Minton AP: Macromolecular crowding: biochemical, and physiological consequences. Annu Rev Biophys Biomol Struct 1993, 22:27-65.
6. 6. Zimmerman SB: Macromolecular crowding effects on macromolecular interactions: some implications for genome structure and function. Biochim Biophys Acta 1993, 1216:175-185.
7. 7. Cole N, Ralston GB: Enhancement of self-association of human spectrin by polyethylene glycol. Int J Biochem 1994, 26:799-804.
8. 8. Lindner R, Raltson G: Effects of dextran on the self-association of human spectrin. Biophys Chem 1995, 57:15-25. An exemplary quantitative characterization and analysis of the effect of excluded volume on macromolecular self-association.
9. 9. Kosk-Kosicka D, Lopez MM, Formitcheva I, Lew VL: Self-association of plasma membrane Ca-ATPase by volume exclusion. FEBS Lett 1995, 371:57-60.
10. 10. Sackett DL, Kosk-Kosicka D: The active species of plasma membrane Ca-ATPase are a dimer and a monomer-calmodulin complex. J Biol Chem 1996, 271:9987-9991.
11. 13Q-NMR off-resonance rotating frame spin-lattice relaxation studies of bovine lens gamma-crystallin self-association: effect of 'macromolecular crowding'. Biochim Biophys Acta 1995, 1246:82-90.
12. 12. Podgornik R, Strey HH, Rau DC, Parsegian VA: Watching molecules crowd: DNA double helices under osmotic stress. Biophys Chem 1995, 57:111-121.
13. 13. Murphy LD, Zimmerman SB: Macromolecular crowding effects on the interaction of DNA with E. coli DNA-binding proteins: a model for bacterial nucleoid stabilization. Biochim Biophys Acta 1994, 1219:277-284.
14. 14. Murphy LD, Zimmerman SB: Condensation and cohesion of lambda DNA in cell extracts and other media: implication for the structure and fuction of DNA in prokaryotes. Biophys Chem 1995, 57:71-92.
15. 15. Zimmerman SB, Murphy LD: Macromolecular crowding and the mandatory condensation of DNA in bacteria. FEBS Lett 1996, 390:245-248.
16. 16. Louie D, Serwer P: Quantification of the effect of excluded volume on double-stranded DNA. J Mol Biol 1994, 242:547-558.
17. 1 7. Reddy MK, Weitzel SE, Von Hippel PH: Assembly of a functional replication complex without ATP hydrolysis: a direct interaction of bacteriophage T4 gp45 with T4 DNA polymerase. Proc Natl Acad Sci USA 1993, 90:3211-3215.
18. 18. Sanders GM, Kassavetis GA, Geiduschek EP: Use of a macromolecular crowding agent to dissect interactions and define functions in transcriptional activation by a DNA-tracking protein: bacteriophage T4 gene 45 protein and late transcription. Proc Natl Acad Sci USA 1994, 92:7703-7707.
19. 19. Madden TL, Herzfeld J: Crowding-induced organization of cytoskeletal elements. I. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles. Biophys J 1993, 65:1147-1154.
20. 20. Madden TL, Herzfeld J: Crowding-induced organization of cytoskeletal elements. II. Dissolution of spontaneously formed filament bundles by capping proteins. J Cell Biol 1994, 126:169-174.
21. 21. Kulp DT, Herzfeld J: Crowding-induced organization of cytoskeletal elements. III. Spontaneous bundling and sorting of self-assembled filaments with different flexibilities. Biophys Chem 1995, 57:93-102.
22. 22. Suzuki A, Yamazaki M, Ito T: Osmoelastic coupling in biological structures: formation of parallel bundles of actin filaments in a crystalline-like structure caused by osmotic stress. Biochemistry 1989, 28:6513-6518.
23. 23. Cuneo P, Magri E, Verzola A, Grazi E: 'Macromolecular crowding' is a primary factor in the organization of the cytoskeleton. Biochem J 1992, 281:507-512.
24. 24. Knull H, Minton AP: Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism. Cell Biochem Funct 1996, in press.
25. 25. Walsh JL, Knull HR: Heteromerous interactions among glycolytic enzymes and of glycolytic enzymes with F-actin: effects of polyethylene glycol. Biochim Biophys Acta 1987, 952:83-91.
26. 26. Knull HR, Walsh JL: Association of glycolytic enzymes with the cytoskeleton. Curr Top Cell Regul 1992, 33:15-30.
27. 27. Agius L: Substrate modulation of aldolase B binding in hepatocytes. Biochem J 1996, 315:651-658.
28. 28. Man J, Herzfeld J: Macromolecular diffusion in crowded solutions. Biophys J 1993, 65:1155-1161.
29. 29. Muramatsu N, Minton AP: Tracer diffusion of globular proteins in concentrated protein solution. Proc Natl Acad Sci USA 1988, 85:2984-2988.
30. 30. Dwyer JD, Bloomfield VA: Brownian dynamics simulations of probe and self-diffusion in concentrated protein and DNA solutions. Biophys J 1993, 65:1810-1816.
31. 31. Dwyer JD, Bloomfield VA: Brownian dynamics simulation of probe diffusion in DNA: effects of probe size, charge and DNA concentrations. Biophys Chem 1995, 57:55-64.
32. 32. Zhou Y, Hall CK: Solute excluded-volume effects on the stability of globular proteins: a statistical-thermodynamic theory. Biopolymers 1996, 38:273-284.
33. 33. Minton AP, Edelhoch H: Light scattering of bovine serum albumin solutions: extension of the hard particle model to allow for electrostatic repulsion. Biopolymers 1982, 21:451-458.
34. 34. Minton AP: A molecular model for the dependence of the osmotic pressure of bovine serum upon concentration and pH. Biophys Chem 1995, 57:65-70.
35. 35. Wills PR, Winzor DJ: Thermodynamic analysis of "preferential solvation" in protein solutions. Biopolymers 1993, 33:1627-1629.
36. 36. Winzor DJ, Wills PR: Thermodynamic nonideality of enzyme solutions supplemented with inert solutes: yeast hexokinase revisited. Biophys Chem 1995, 57:103-110. A reinterpretation, in the context of excluded volume theory, of the data presented in [38].
37. 37. Winzor DJ, Wills PR: Thermodynamic nonideality and protein solvation. In Protein-Solvent Interactions. Edited by Gregory RB. New York: Marcel Dekker; 1995:483-520.
38. 38. Rand R, Fuller NL, Butko P, Francis G, Nicholls P: Measured change in protein solvation with substrate binding and turnover. Biochemistry 1993, 32:5925-5929.
39. 39. Minton AP: Macromolecular crowding and molecular recognition. J Mol Recognit 1993, 6:211-214.
40. 40. Minton AP, Colclasure GC, Parker JC: Model for the role of macromolecular crowding in regulation of cellular volume. Proc Natl Acad Sci USA 1992, 89:10504-10506.
41. 41. Minton AP: Influence of macromolecular crowding on intracellular association reactions: possible role in volume regulation. In Cellular and Molecular Physiology of Cell Volume Regulation. Edited by Strange K. Boca Raton: CRC Press; 1993:181-190.
42. 42. Parker JC, Dunham PB, Minton AP: Effects of ionic strength on the regulation of Na/H exchange and K-Cl cotransport in dog red blood cells. J Gen Physiol 1995, 105:677-699.
43. 43. Garner MM, Burg MB: Macromolecular crowding and confinement in cells exposed to hypertonicity. Am J Physiol 1994, 266:C877-C892.
44. 44. Wills PR, Georgalis Y, DiJk J, Winzor DJ: Measurement of thermodynamic nonideality arising from volume-exclusion interactions between proteins and polymers. Biophys Chem 1995, 57:37-46.