Mutational analysis of Ser14 and Asp157 in the nucleotide-binding site of β-actin

European Journal of Biochemistry

Volumn 265, Issue 1, 1999, Pages 210-220

  Schüler, Herwig ^c   Korenbaum, Elena ^b   Schutt, Clarence E ^c   Lindberg, Uno ^a   Karlsson, Roger ^c  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b UNIVERSITY OF COLOGNE   (Germany)

^c NONE

Author keywords

actin mutants; ATP hydrolysis; Polymerization; Profilin; Thermal stability

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ASPARTIC ACID; BETA ACTIN; PROFILIN; SERINE;

ACTIN POLYMERIZATION; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEIN NUCLEIC ACID INTERACTION; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; THERMOSTABILITY;

ACTINS; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ANIMALS; ASPARTIC ACID; CALCIUM; CATALYTIC DOMAIN; CATIONS; CHICKENS; CONTRACTILE PROTEINS; DEOXYRIBONUCLEASE I; ENZYME STABILITY; HEAT; HYDROLYSIS; MAGNESIUM; MICROFILAMENT PROTEINS; MODELS, MOLECULAR; MUTATION; MYOSINS; POTASSIUM; PROFILINS; PROTEIN BINDING; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SERINE;

EID: 0342504193     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00716.x     Document Type: Article

References (74)

1. 1. Asakura, S. (1961) The interaction between G-actin and ATP. Arch. Biochem. Biophys. 92, 140-149.
2. 2. Strohman, R.C. & Samorodin, A.J. (1962) The requirements for adenosine triphosphate binding to globular actin. J. Biol. Chem. 237, 363-370.
3. 3. Higashi. S. & Oosawa, F. (1965) Conformational changes associated with polymerization and nucleotide binding in actin molecules. J. Mol. Biol. 12, 843-865.
4. 4. Cooke, R. & Murdoch, L. (1973) Interaction of actin with analogs of adenosine triphosphate. Biochemistry 12, 3927-3932.
5. +-induced actin assembly. J. Cell Biol. 93, 648-654.
6. 6. Carlier, M.-F., Pantaloni, D. & Korn, E.D. (1984) Evidence for an ATP cap at the ends of actin filaments and its regulation of the F-actin steady state. J. Biol. Chem. 259, 9983-9986.
7. 7. Korn, E.D., Carlier, M.-F. & Pantaloni, D. (1987) Actin polymerization and ATP hydrolysis. Science 238, 638-644.
8. 8. Schutt, C.E. & Lindberg, U. (1998) Muscle contraction as a Markov process I: energetics of the process. Acta Physiol. Scand. 163, 307-324.
9. 9. Kabsch, W., Mannherz, H.G., Suck, D., Pai, E.F. & Holmes, K.C. (1990) Atomic structure of the actin: DNase I complex. Nature 347, 37-44.
10. 10. McLaughlin, P.J., Gooch, J.T., Mannherz, H.G. & Weeds, A.G. (1993) Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364, 685-692.
11. 11. Schutt, C.E., Myslik, J.C., Rozycki, M.D., Goonesekere, N.C.W. & Lindberg, U. (1993) The structure of crystalline profilin-beta-actin. Nature 365, 810-816.
12. 12. Chik, J.K., Lindberg, U. & Schutt, C.E. (1996) The structure of an open state of beta-actin at 2.65 Å resolution. J. Mol. Biol. 263, 607-623.
13. 13. Page, R., Lindberg, U. & Schutt, C.E. (1998) Domain motions in actin. J. Mol. Biol. 280, 463-474.
14. 14. Mannherz, H.G., Goody, R.S., Konrad, M. & Nowak, E. (1980) The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin. Eur. J. Biochem. 104, 367-379.
15. 15. Mockrin, S.C. & Korn, E.D. (1980) Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry 19, 5359-5362.
16. 16. Goldschmidt-Clermont, P.J., Machesky, L.M., Doberstein, S.K. & Pollard, T.D. (1991) Mechanism of the interaction of human platelet profilin with actin. J. Cell Biol. 113, 1081-1089.
17. 17. Korenbaum, E., Nordberg, P., Björkegren-Sjögren, C., Schutt, C.E., Lindberg, U. & Karlsson, R. (1998) The role of profilin in actin polymerization and nucleotide exchange. Biochemistry 37, 9274-9283.
18. 18. Rozycki, M.D., Myslik, J.C., Schutt, C.E. & Lindberg, U. (1994) Structural aspects of actin-binding proteins. Curr. Opin. Cell Biol. 6, 87-95.
19. 19. Frieden, C., Lieberman, D. & Gilbert, H.R. (1980) A fluorescent probe for conformational changes in skeletal muscle G-actin. J. Biol. Chem. 255, 8991-8993.
20. 2+-induced conformational change requires ATP. Biochemistry 24, 4192-4196.
21. 21. Crosbie, R.H., Miller, C., Cheung, P., Goodnight, T., Muhlrad, A. & Reisler, E. (1994) Structural connectivity in actin: effect of C-terminal modifications on the properties of actin. Biophys. J. 67, 1957-1964.
22. 22. Muhlrad, A., Cheung, P., Phan, B.C., Miller, C. & Reisler, E. (1994) Dynamic properties of actin. Structural changes induced by beryllium fluoride. J. Biol. Chem. 269, 11852-11858.
23. 23. Strzelecka-Golaszewska. H., Mossakowska, M., Wozniak, A., Moraczewska, J. & Nakayama, H. (1995) Long-range conformational effects of proteolytic removal of the last three residues of actin. Biochem. J. 307, 527-534.
24. 24. Sheterline, P., Clayton, J. & Sparrow, J. (1996) Actin. Protein Profile 3, 1-116.
25. 25. Myslik, J.C. (1992) The structure of actin in the crystalline profilin:actin complex. Ph.D. Thesis, Princeton University.
26. 26. Flaherty, K.M., McKay, D.B., Kabsch, W. & Holmes. K.C. (1991) Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc. Natl Acad. Sci. USA 88, 5041-5045.
27. 27. Chen, X. & Rubenstein, P.A. (1995) A mutation in an ATP-binding loop of Saccharomyces cerevisiae actin (S14A) causes a temperature-sensitive phenotype in vivo and in vitro. J. Biol. Chem. 270, 11406-11414.
28. 28. Chen, X., Peng, J., Pedram, M., Swenson, C.E. & Rubenstein, P.A. (1995) The effect of the S14A mutation on the conformation and thermostability of Saccharomyces cerevisiae G-actin and its interaction with adenine nucleotides. J. Biol. Chem. 270, 11415-11423.
29. 29. Orlova, A., Chen, X., Rubenstein, P.A. & Egelman, E.H. (1997) Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft. J. Mol. Biol. 271, 235-243.
30. 30. Wertman, K., Drubin, D.G. & Botstein, D. (1992) Systematic mutational analysis of the yeast ACT1 gene. Genetics 132, 337-350.
31. 31. Schüler, H., Korenbaum, E., Lindberg, U. & Karlsson, R. (1997) Studies on the ATP-binding site of actin using site-directed mutagenesis. In Interacting Protein Domains: Their Role in Signal and Energy Transduction (Heilmeyer, L., ed.), pp. 255-258. Springer-Verlag, Heidelberg.
32. 32. Carlsson, L., Markey, F., Blikstad, I., Persson, T. & Lindberg, U. (1979) Reorganization of actin in platelets stimulated by thrombin as measured by the DNase I inhibition assay. Proc. Natl Acad. Sci. USA 76, 6376-6380.
33. 33. Kunkel, T.A., Roberts, T.T. & Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
34. 34. Karlsson, R. (1988) Expression of chicken beta-actin in Saccharomyces cerevisiae. Gene 68, 249-257.
35. 35. Aspenström, P., Schutt, C.E., Lindberg, U. & Karlsson, R. (1993) Mutations in beta-actin: influence on polymer formation and on interactions with myosin and profilin. FEBS Lett. 329, 163-170.
36. 36. Lazarides, E. & Lindberg, U. (1974) Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc. Natl Acad. Sci. USA 71, 4742-4746.
37. 37. Houk, T.W. & Ue, K. (1974) The measurement of actin concentration in solution: a comparison of methods. Anal. Biochem. 62, 66-74.
38. 38. Gershman, L.C., Newman, J., Selden, L.A. & Estes, J.E. (1984) Boundcation exchange affects the lag phase in actin polymerization. Biochemistry 23, 2199-2203
39. 39. Lindberg, U., Schutt, C.E., Hellsten, E., Tjäder, A.-C. & Hult, T. (1988) The use of poly (L-proline)-Sepharose in the isolation of profilin and profilactin complexes. Biochim. Biophys. Acta 967, 391-400.
40. 40. Perry, S.V. (1955) Myosin adenosinetriphosphatase. Methods Enzymol. 2, 582-588.
41. 41. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
42. 42. Gimona, M., Vandekerckhove, J., Goethals, M., Herzog, M., Lando, Z. & Small, J.V. (1994) Beta-actin specific monoclonal antibody. Cell Motil. Cytoskeleton 27, 108-116.
43. 2+ to actin without loss of polymerizability: the involvement of the rapidly reacting-SH group. Arch. Biochem. Biophys. 150, 164-174.
44. 2+-binding to actin upon removal of the C-terminal phenylalanine by carboxypeptidase A. Arch. Biochem. Biophys. 181, 359-361.
45. 45. Secrist, J.A., III, Barrio, J.R. & Leonard, N.J. (1972) A fluorescent modification of adenosine triphosphate with activity in enzyme systems: I,N6-ethenoadenosine triphosphate. Science 175, 646-647.
46. 46. Waechter, F. & Engel, J. (1975) The kinetics of the exchange of G-actin-bound I: N6-ethenoadenosine 5′-triphosphate with ATP as followed by fluorescence. Eur. J. Biochem. 57, 453-459.
47. 47. Spudich, J.A. (1974) Biochemical and structural studies of actomyosin-like proteins from non-muscle cells. II. Purification, properties and membrane association of actin from amoebae of Dictyostelium discoideum. J. Biol. Chem. 249, 6013-6020.
48. 48. Blikstad, I., Markey, F., Carlsson, L., Persson, T. & Lindberg, U. (1978) Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell 15, 935-943.
49. 2+ on the thermal denaturation of carboxy-peptidase B. Biochemistry 30, 2067-2072.
50. 50. Kouyama, T. & Mihashi, K. (1981) Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114, 33-38.
51. 51. Kron, SJ. & Spudich, J.A. (1986) Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl Acad. Sci. USA 83, 6272-6276.
52. 52. Kishino, A. & Yanagida, T. (1988) Force measurements by micro-manipulation of a single actin filament by glass needles. Nature 334, 74-76.
53. 53. Gorbunoff, M.J. & Timasheff, S.N. (1984) The interaction of proteins with hydroxyapatite. III. Mechanism. Anal. Biochem. 136, 440-445.
54. 54. Malm, B. (1984) Chemical modification of Cys-374 of actin interferes with the formation of the profilactin complex. FEBS Lett. 173, 399-402.
55. 55. Le Bihan, T. & Gicquaud, C. (1993) Kinetic study of the thermal denaturation of G actin using differential scanning calorimetry and intrinsic fluorescence spectroscopy. Biochem. Biophys. Res. Comm. 194, 1065-1073.
56. 56. Aspenström, P., Engkvist, H., Lindberg, U. & Karlsson, R. (1992) Characterization of yeast-expressed beta-actins, site-specifically mutated at the tumor-related residue Gly245. Eur. J. Biochem. 207, 315-320.
57. 57. Selden, L.A., Estes, J.E. & Gershman, L.C. (1983) The tightly bound divalent cation regulates actin polymerization. Biochem. Biophys. Res. Comm. 116, 478-485.
58. 58. Frieden, C. & Patane, K. (1988) Mechanism for nucleotide exchange in monomeric actin. Biochemistry 27, 3812-3820.
59. 59. Selden, L.A., Kinosian, H.J., Estes, J.E. & Gershman, L.C. (1999) Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics. Biochemistry 38, 2769-2778.
60. 60. Geffrey, G.A. & Sanger, W. (1994) Hydrogen Bonding in Biological Structures. Springer-Verlag, Heidelberg.
61. 61. Creighton, T.E. (1993) Proteins: Structures and Molecular Properties, 2nd edn. W. H. Freeman, New York, USA.
62. 62. Stuckey, J.A., Schubert, H.L., Fauman, E.B., Zhang, Z.-Y., Dixon, J.E. & Saper, M.A. (1994) Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate. Nature 370, 571-575.
63. 63. Su, X.-D., Taddei, N., Stefani, M., Ramponi, G. & Nordlund, P. (1994) The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature 370, 575-578.
64. 64. Schnetz, K., Sutrina, S.L., Saier, M.H. Jr. & & Rak, B. (1990) Identification of catalytic residues in the beta-glucoside permease of Escherichia coli by site-specific mutagenesis and demonstration of interdomain cross-reactivity between the beta-glucoside and glucose systems. J. Biol. Chem. 265, 13464-13471.
65. 65. van Montford, R.L.M., Pijning, T., Kalk, K.H., Reizer, J., Saier, M.H., Jr., Thunnissen, M.M.G.M., Robillard, G.T. & Dijkstra, B.W. (1997) The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure 5, 217-225.
66. 4. Biochemistry 34, 8960-8972.
67. 67. O'Brien, M.C., Flaherty, K.M. & McKay, D.B. (1996) Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis. J. Biol. Chem. 271, 15874-15878.
68. 68. Wilbanks, S.M. & McKay, D.B. (1995) How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270, 2251-2257.
69. 69. Schweins, T., Geyer, M., Scheffzek, K., Warshel, A., Kalbitzer, H.R. & Wittinghofer, A. (1995) Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins. Nat. Struct. Biol. 2, 36-44.
70. 70. Smith, C.A. & Rayment, I. (1996) Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys. J. 70, 1590-1602.
71. 71. Sprang, S.R. (1997) G proteins, effectors and GAPs: structure and mechanism. Curr. Opin. Struct. Biol. 7, 849-856.
72. 72. Stock, A.M., Martinez-Hackart, E., Rasmussen, B.F., West, A.H., Stock, J.B., Ringe, D. & Petsko, G.A. (1993) Structure of the Mg (2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry 32, 13375-13380.
73. 73. Gordon, D.J., Boyer, J.L. & Korn, E.D. (1977) Comparative biochemistry of non-muscle actins. J. Biol. Chem. 252, 8300-8309.
74. 74. Hitchcock, S.E., Carlsson, L. & Lindberg, U. (1976) Depolymerization of F-actin by deoxyribonuclease I. Cell 7, 531-542.