Mechanism of actin polymerization by myosin subfragment-1 probed by dynamic light scattering

Bioelectrochemistry

Volumn 70, Issue 1, 2007, Pages 53-57

  Galinska Rakoczy A ^a   Jachimska, Barbara ^b   Strzelecka Golaszewska H ^a  

^a NENCKI INSTITUTE OF EXPERIMENTAL BIOLOGY   (Poland)

^b INSTITUTE OF CATALYSIS AND SURFACE CHEMISTRY   (Poland)

Author keywords

Actin; Actin polymerization; Myosin subfragment 1

Indexed keywords

IONIC STRENGTH; LIGHT SCATTERING; NUCLEATION; OLIGOMERS; POLYMERIZATION; REACTION KINETICS; SODIUM CHLORIDE;

ACTIN POLYMERIZATION; FILAMENT GROWTH; HELICAL FILAMENTS; HELICAL FILAMENTS HELICAL FILAMENTS;

MONOMERS;

ACTIN; ADENOSINE TRIPHOSPHATE; G ACTIN; MYOSIN SUBFRAGMENT 1;

ARTICLE; COMPLEX FORMATION; LIGHT SCATTERING; NONHUMAN; PARTICLE SIZE; POLYMERIZATION; RABBIT; SKELETAL MUSCLE;

ACTINS; ANIMALS; MYOSIN SUBFRAGMENTS; PARTICLE SIZE; RATS; SPECTRUM ANALYSIS;

EID: 33845680986     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2006.03.035     Document Type: Article

References (34)

1. Carlier M.-F. Actin: protein structure and filament dynamics. J. Biol. Chem. 266 (1991) 1-4
2. Carlier M.-F., and Pantaloni D. Control of actin dynamics in cell motility. J. Mol. Biol. 269 (1997) 459-467
3. Pollard T.D., Blanchoin L., and Mullins R.D. Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biomol. Struct. 29 (2000) 545-576
4. Chaussepied P., and Kasprzak A.A. Change in the actin-myosin subfragment 1 interaction during actin polymerization. J. Biol. Chem. 264 (1989) 20752-20759
5. Lheureux K., and Chaussepied P. Comparative studies of the monomeric and filamentous actin-myosin head complexes. Biochemistry 34 (1995) 11435-11444
6. Combeau C., Didry D., and Carlier M.-F. Interaction between G-actin and myosin subfragment-1 probed by covalent cross-linking. J. Biol. Chem. 267 (1992) 14038-14046
7. Weeds A.G., and Lowey S. Substructure of the myosin molecule. II. The light chains of myosin. J. Mol. Biol. 61 (1971) 701-725
8. Weeds A.G., and Taylor R.S. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature 257 (1975) 54-56
9. Soldati T. Unconventional myosins, actin dynamics and endocytosis: a ménage à trois?. Traffic 4 (2003) 358-366
10. Tawada K., and Oosawa F. Activation of H-meromyosin ATPase by polymers of actin and carboxymethylated actin. J. Mol. Biol. 44 (1969) 309-317
11. Offer G., Baker H., and Baker L. Interaction of monomeric and polymeric actin with myosin subfragment 1. J. Mol. Biol. 66 (1972) 435-444
12. Estes J.E., and Gershman L.C. Activation of heavy meromyosin adenosine triphosphatase by various states of actin. Biochemistry 17 (1978) 2495-2499
13. Chaussepied P., and Kasprzak A.A. Isolation and characterization of the G-actin-myosin head complex. Nature 342 (1989) 950-953
14. Chen T., and Reisler E. Interactions of myosin subfragment-1 isozymes with G-actin. Biochemistry 30 (1991) 4546-4552
15. Lheureux K., Forné T., and Chaussepied P. Interaction and polymerization of the G-actin-myosin head complex - effect of DNase-I. Biochemistry 32 (1993) 10005-10014
16. Miller L., Phillips M., and Reisler E. Polymerization of G-actin by myosin subfragment 1. J. Biol. Chem. 263 (1988) 1996-2002
17. Chen T., Heigentz M., and Reisler E. Myosin subfragment-1 and structural elements of G-actin - effects of S-1(A2) on sequences 39-52 and sequences 61-69 in subdomain-2 of G-actin. Biochemistry 31 (1992) 2941-2946
18. Valentin-Ranc C., Combeau C., Carlier M.-F., and Pantaloni D. Myosin subfragment-1 interacts with two G-actin molecules in the absence of ATP. J. Biol. Chem. 266 (1991) 17872-17879
19. Valentin-Ranc C., and Carlier M.-F. Characterization of oligomers as kinetic intermediates in myosin subfragment 1-induced polymerization of G-actin. J. Biol. Chem. 267 (1992) 21543-21550
20. 1-decorated filaments. Biochemistry 36 (1997) 11843-11850
21. Spudich J.A., and Watt S. The regulation of skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246 (1971) 4866-4871
22. Margossian S.S., and Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85 (1982) 55-71
23. Trayer H.R., and Trayer I.P. Preparation of myosin and its subfragments from rabbit skeletal muscle. Biochemistry 27 (1988) 5718-5727
24. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
25. Houk W.T., and Ue K. The measurement of actin concentration in solution: a comparison of methods. Anal. Biochem. 62 (1974) 66-74
26. Rayment I., Rypniewski W.R., Schmidt-Bäse K., Smith R., Tomchick D.R., Benning M.W., Winkelmann D.A., Wasenberg G., and Holden H.M. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261 (1993) 50-58
27. Kabsch W., Mannherz H.G., Suck D., Pai E.F., and Holmes K.C. Atomic structure of the actin:DNase I complex. Nature 347 (1990) 37-44
28. Rayment I., Holden H.M., Whittaker M., Yohn C.B., Lorenz M., Holmes K.C., and Milligan R.A. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261 (1993) 58-65
29. Milligan R.A. Protein-protein interaction in the rigor actomyosin complex. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 21-26
30. Hanson J., and Lowy J. The structure of F-actin and of actin filaments isolated from muscle. J. Mol. Biol. 6 (1963) 46-60
31. Holmes K.C., Popp D., Gebhard D., and Kabsch W. Atomic model of the actin filament. Nature 347 (1990) 44-49
32. Moore P.B., Huxley H.E., and DeRosier D.J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J. Mol. Biol. 50 (1970) 279-295
33. Blanchoin L., Fievez S., Travers F., Carlier M.-F., and Pantaloni D. Kinetics of the interaction of myosin subfragment-1 with G-actin. Effect of nucleotides and DNase I. J. Biol. Chem. 270 (1995) 7125-7133
34. Sept D., and McCammon J.A. Thermodynamics and kinetics of actin filament nucleation. Biophys. J. 81 (2001) 667-674