Thymosin-β4 changes the conformation and dynamics of actin monomers

Biophysical Journal

Volumn 78, Issue 5, 2000, Pages 2516-2527

  De La Cruz, Enrique M ^a   Ostap, E Michael ^a   Brundage, Rodney A ^b   Reddy, K S ^a   Sweeney, H Lee ^a   Safer, Daniel ^a,b  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; CALCIUM ION; CYSTEINE; GLYCINE; THYMOSIN BETA4;

ARTICLE; CIRCULAR DICHROISM; CROSS LINKING; ENTHALPY; ENTROPY; KINETICS; OXIDATIVE STRESS; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION;

METAZOA; TRITIUM;

EID: 0034121422     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76797-X     Document Type: Article

References (56)

1. Anderson, N. G. 1970. In CRC Handbook of Biochemistry, Selected Data for Molecular Biology, 2nd Ed. H. A. Sober, editor. CRC Press, Boca Raton, FL. J288-J291.
2. 4 on actin by competition with G-actin binding proteins indicates negative co-operativity between binding sites located on opposite subdomains of actin. Biochem. J. 327:787-793.
3. 2+ exchange as detected by proton NMR spectroscopy. Eur. J. Biochem. 146:5-8.
4. Buttle, D. J. 1994. Glycyl endopeptidase. Methods Enzymol. 244:539-555.
5. 4 is not a simple G-actin sequestering protein and interacts with F-actin at high concentrations. J. Biol. Chem. 271:9231-9239.
6. 4 by the ATP/ADP ratio: possible implication in the regulation of actin dynamics. Proc. Natl. Acad. Sci. USA. 90:5034-5038.
7. Carlier, M.-F., D. Pantaloni, and E. D. Korn. 1986. Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin. J. Biol. Chem. 261:10778-10784.
8. Chik, J. K., U. Lindberg, and C. E. Schutt. 1996. The structure of an open state of beta-actin at 2.65 Å resolution. J. Mol. Biol. 263:607-623.
9. r. Nature Struct. Biol. 4:849-853.
10. 4 in water determined by NMR spectroscopy. Eur. J. Biochem. 218:335-344.
11. De La Cruz, E. M., and T. D. Pollard. 1996. Kinetics and thermodynamics of phalloidin binding to actin filaments from three divergent species. Biochemistry. 35:14054-14061.
12. Englander, S. W., and J. J. Englander. 1972. Hydrogen-tritium exchange. Methods Enzymol. 26:406-413.
13. Eyring, H. 1935. The activated complex and the absolute rate of chemical reactions. Chem. Rev. 17:65-77.
14. Fischer, S., and C. S. Verma. 1999. Binding of buried structural water increases the flexibility of proteins. Proc. Natl. Acad. Sci. USA. 96:9613-9615.
15. Frieden, C., D. Lieberman, and H. R. Gilbert. 1980. A fluorescent probe for conformational changes in skeletal muscle G-actin. J. Biol. Chem. 255:8991-8993.
16. 2+-induced conformational change requires ATP. Biochemistry. 24:4192-4196.
17. Fuller, N., and R. P. Rand. 1999. Water in actin polymerization. Biophys. J. 76:3261-3266.
18. Gaszner, B., M. Nyitrai, N. Hartvig, T. Koszegi, B. Somogyi, and J. Belagyi. 1999. Replacement of ATP with ADP affects the dynamic and conformational properties of actin monomer. Biochemistry. 38:12885-12892.
19. 4 and profilin: a potential regulatory mechanism for actin polymerization in cells. Mol. Biol. Cell. 3:1015-1024.
20. Gutfreund, H. 1995. Kinetics for the Life Sciences. Cambridge University Press, Cambridge, UK.
21. 4-like peptides as assessed by the DNase I inhibition assay. Biol. Chem. Hoppe-Seyler. 374:117-122.
22. 9. FEBS Lett. 329:9-12.
23. Holmes, K. C., D. Popp, W. Gebhard, and W. Kabsch. 1990. Atomic model of the actin filament. Nature. 347:44-49.
24. Houk, T. W., and K. Ue. 1974. The measurement of actin concentration in solution: a comparison of methods. Anal. Biochem. 62:66-74.
25. Huang, Z., R. P. Haugland, W. M. You, and R. P. Haugland. 1992. Phallotoxin and actin binding assay by fluorescence enhancement. Anal. Biochem. 200:199-204.
26. Huff, T., D. Zerzawy, and E. Hannappel. 1995. Interactions of beta-thymosins, thymosin beta 4-sulfoxide, and N-terminally truncated thymosin beta 4 with actin studied by equilibrium centrifugation, chemical cross-linking and viscometry. Eur. J. Biochem. 230:650-657.
27. met. J. Muscle Res. Cell Motil. 15:278-286.
28. Kabsch, W., H.-G. Mannherz, D. Suck, E. F. Pai, and K. C. Holmes. 1990. Atomic structure of the actin:DNase I complex. Nature. 347:37-44.
29. Kim, E., M. Motoki, K. Seguro, A. Muhlrad, and E. Reisler. 1995. Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41. Biophys. J. 69:2024-2032.
30. Kinosian, H. J., L. A. Selden, J. E. Estes, and L. C. Gershman. 1993. Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates. J. Biol. Chem. 268:8683-8691.
31. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
32. Lee, J. C., and S. N. Timasheff. 1981. The stabilization of proteins by sucrose. J. Biol. Chem. 256:7193-7201.
33. Lehrer, S. S., and G. Kerwar. 1972. Intrinsic fluorescence of actin. Biochemistry. 11:1211-1217.
34. MacLean-Fletcher, S., and T. D. Pollard. 1980. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem. Biophys. Res. Commun. 96:18-27.
35. McLaughlin, P. J., J. T. Gooch, H.-G. Mannherz, and A. G. Weeds. 1993. Structure of gelsolin segment-1 actin complex and the mechanism of filament severing. Nature. 364:685-692.
36. Moraczewska, J., H. Strzelecka-Golaszewska, P. D. J. Moens, and C. G. dos Remedies. 1996. Structural changes in subdomain 2 of G-actin observed by fluorescence spectroscopy. Biochem. J. 317:605-611.
37. Murphy, A. J. 1971. Circular dichroism of the adenine and 6-mercaptopurine nucleotide complexes of actin. Biochemistry. 10:3723-3728.
38. Pardee, J. D., and J. A. Spudich. 1982. Purification of muscle actin. Methods Enzymol. 85:164-181.
39. Parsegian, V. A., R. P. Rand, and D. C. Rau. 1995. Macromolecules and water: probing with osmotic stress. Methods Enzymol. 259:43-94.
40. Pollard, T. D. 1984. Polymerization of ADP actin. J. Cell Biol. 99:769-777.
41. Qin, L., and D. K. Srivastava. 1998. Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-CoA, to medium-chain acyl- coenzyme-A dehydrogenase. Biochemistry. 37:3499-3508.
42. Rand, R. P., N. L. Fuller, P. Butko, G. Francis, and P. Nicholls. 1993. Measured change in protein solvation with substrate binding and turnover. Biochemistry: 32:5925-5929.
43. 4. FEBS Lett. 387:132-136.
44. 4 complex initiated by the addition of actin nuclei, nuclei stabilizing agents or myosin S1. FEBS Lett. 347:247-250.
45. 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. Biochemistry. 36:5806-5816.
46. Schutt, C. E., J. C. Myslik, M. D. Rozycki, N. C. W. Goonesekere, and U. Lindberg. 1993. The structure of crystalline profilin-β-actin. Nature. 365:810-816.
47. Schwarz, G. 1965. On the kinetics of the helix-coil transition of polypeptides in solution. J. Mol. Biol. 11:64-67.
48. Strzelecka-Golaszewska, H., J. Moraczewska, S. Y. Khaitlina, and M. Mossakowska. 1993. Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion. Eur. J. Biochem. 211:731-742.
49. Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA. 82:1074-1078.
50. Tirion, M. M., and D. ben-Avraham. 1993. Normal mode analysis of G-actin. J. Mol Biol. 230:186-195.
51. Vinson, V. K., E. M. De La Cruz, H. N. Higgs, and T. D. Pollard. 1998. Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry. 37:10871-10880.
52. Wang, A., A. D. Robertson, and D. W. Bolen. 1995. Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A. Biochemistry. 34:15096-15104.
53. 4 with muscle and platelet actin: implications for actin sequestration in resting platelets. Biochemistry. 31:6179-6185.
54. Williams, S., T. P. Causgrove, R. Gilmanshjn, K. S. Fang, R. H. Callendar, W. H. Woodruff, and R. B. Dyer. 1996. Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry. 35:691-697.
55. Wolf, A. V., M. G. Brown, and P. C. Prentiss. 1986. In CRC Handbook of Chemistry and Physics. R. T. Weast, editor. CRC Press, Boca Raton, FL. D219, D262.
56. 4 are both actin monomer sequestering proteins. J. Biol. Chem. 268:502-509.