The structure of the head-tail junction of the myosin molecule

Journal of Molecular Biology

Volumn 256, Issue 3, 1996, Pages 407-416

  Offer, Gerald ^a   Knight, Peter ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

Energy minimisation; Flexibility; Molecular dynamics; Regulation; helical coiled coil

Indexed keywords

MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; PROLINE;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE;

EID: 0029870409     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0096     Document Type: Editorial

References (44)

1. Ankrett, R. J., Rowe, A. J., Cross, R. A., Kendrick-Jones, J. & Bagshaw, C. R. (1991). A folded (10 S) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity. J. Mol. Biol. 217, 323-335.
2. Bagshaw, C. R. (1980). Divalent metal binding and subunit interactions in myosins: a critical review. J. Muscle Res. Cell Motil. 1, 255-277.
3. Barlow, D. J. & Thornton, J. M. (1988). Helix geometry in proteins. J. Mol. Biol. 201, 601-619.
4. Barouch, W. W., Breese, K. E., Davidoff, S., Leszyk, J., Szent-Györgyi, A. G., Theibert, J. L. & Collins, J. H. (1991). Amino acid sequences of myosin essential and regulatory light chains from two clam species: comparison with other molluscan myosin light chains. J. Muscle Res. Cell Motil. 12, 321-332.
5. Chantler, P. D. & Bower, S. M. (1988). Cross-linking between two translationally equivalent sites on the two heads of myosin. J. Biol. Chem. 263, 938-944.
6. Chantier, P. D. & Tao, T. (1986). Interhead fluorescence energy transfer between probes attached to translationally equivalent sites on the regulatory light chains of scallop myosin. J. Mol. Biol. 192, 87-99.
7. Chantler, P. D., Sellers, J. R. & Szent-Györgyi, A. G. (1981). Cooperativity in scallop myosin. Biochemistry, 20, 210-216.
8. Collins, J. H. (1991). Myosin light chains and troponin C: structural and evolutionary relationships revealed by amino acid sequence comparisons. J. Muscle Res. Cell Motil. 12, 3-25.
9. Craig, R., Smith, R. & Kendrick-Jones, J. (1983). Light chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules. Nature, 302, 436-439.
10. Eads, T. M., Thomas, D. D. & Austin, R. H. (1984). Microsecond rotational motions of eosin-labeled myosin measured by time-resolved anisotropy of absorption and phosphorescence. J. Mol. Biol. 179, 55-81.
11. Ellenberger, T. E., Brandi, C. J., Struhl, K. & Harrison, S. C. (1992). The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α helices: crystal structure of the protein-DNA complex. Cell 71, 1223-1237.
12. Elliott, A. & Offer, G. (1978). Shape and flexibility of the myosin molecule. J. Mol. Biol. 123, 505-519.
13. 2+ and ATP. J. Cell Biol. 109, 529-538.
14. 2+ and ATP. J. Muscle Res. Cell Motil. 13, 436-446.
15. Hardwicke, P. M. D. & Szent-Györgyi, A. G. (1985). Proximity of regulatory light chains in scallop myosin. J. Mol. Biol. 183, 203-211.
16. Huxley, H. E. (1969). The mechanism of muscular contraction. Science, 164, 1356-1366.
17. Karn, J., Brenner, S. & Barnett, L. (1983). Protein structural domains in the Caenorhabditis elegans unc-54 myosin heavy chain gene are not separated by introns. Proc. Natl Acad. Sci. USA, 80, 4253-4257.
18. Knight, P. J. (1996). Dynamic behaviour of the head-tail junction of myosin. J. Mol. Biol. 225, 269-274.
19. Knight, P. & Trinick, J. (1984). Structure of the myosin projections on native thick filaments from vertebrate skeletal muscle. J. Mol. Biol. 177, 461-482.
20. Kwon, H., Melandri, F. D. & Szent-Györgyi, A. G. (1992). Role of gizzard myosin light chains in calcium binding. J. Muscle Res. Cell Motil. 13, 315-320.
21. McLachlan, A. D. & Karn, J. (1982). Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature, 299, 226-231.
22. Mendelson, R. A., Morales, M. F. & Botts, J. (1973). Segmental flexibility of the S-1 moiety of myosin. Biochemistry, 12, 2250-2255.
23. Nyitray L., Goodwin, E. B. & Szent-Györgyi, A. G. (1991). Complete primary structure of a scallop striated muscle myosin heavy chain. J. Biol. Chem. 266, 18469-18476.
24. Offer, G. (1990). Skip residues correlate with bends in the myosin tail. J. Mol. Biol. 216, 213-218.
25. Offer, G. & Elliott, A. (1978). Can a myosin molecule bind to two actin filaments? Nature, 271, 325-329.
26. Offer, G. & Sessions, R. (1995). Computer modelling of the α-helical coiled coil. Packing of side chains in the inner core. J. Mol. Biol. 249, 967-987.
27. Onishi, H. & Wakabayashi, T. (1982). Electron microscopic studies of myosin molecules from chicken gizzard muscle. 1. the formation of the intramolecular loop in the myosin tail. J. Biochem. 92, 871-879.
28. Persecchini, A. & Hartshorne, D. J. (1981). Phosphorylation of smooth muscle myosin: evidence for cooperativity between the heads. Science, 213, 1383-1385.
29. Quinlan, R. A. & Stewart, M. (1987). Crystalline tubes of myosin subfragment-2 showing the coiled-coil and molecular interaction geometry J. Cell Biol. 105, 403-415.
30. Rayment, I., Rypniewski, W. R., Schmidt-Base, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G. & Holden, H. M. (1993a). Three-dimensional structure of myosin subfragment-1: a molecular motor. Science, 261, 50-58.
31. Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M., Holmes, K. C. & Milligan, R. A. (1993b). Structure of the actin-myosin complex and its implications for muscle contraction. Science, 261, 58-65.
32. Rimm, D. L., Sinard, J. H. & Pollard, T. D. (1989). Location of the head-tail junction of myosin. J. Cell Biol. 108, 1783-1789.
33. Slayter, H. S. & Lowey S. (1967). Substructure of the myosin molecule as visualized by electron microscopy. Proc. Natl Acad. Sci. USA, 58, 1611-1618.
34. Stafford, W. F., Szentkiralyi, E. M. & Szent-Györgyi, A. G. (1979). Regulatory properties of single-headed fragments of scallop myosin. Biochemistry, 18, 5273-5280.
35. Suzuki, H., Stafford, W. F., Slayter, H. S. & Seidel, J. C. (1985). A conformational transition in gizzard heavy meromyosin involving the head-tail junction resulting in changes in sedimentation coefficient, ATPase activity, and orientation of heads. J. Biol. Chem. 260, 14810-14817.
36. Szent-Györgyi, A. G. & Chantler, P. D. (1994). Control of contraction by calcium binding to myosin. In Myology (Engel, A. G. & Franzini-Armstrong, C. eds), pp. 506-528, McGraw-Hill, New York.
37. Takahashi, K. (1978). Topography of the myosin molecule as visualized by an improved negative staining method. J. Biochem. 83, 905-908.
38. Trybus, K. M. (1994a). Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length. J. Biol. Chem. 269, 20819-20822.
39. Trybus, K. M. (1994b). Role of myosin light chains. J. Muscle Res. Cell Motil. 15, 587-594.
40. Trybus, K. M., Huiatt, T. W. & Lowey S. (1982). A bent monomeric conformation of myosin from smooth muscle. Proc. Natl Acad. Sci. USA, 79, 6151-6155.
41. Walker, M., Knight, P. & Trinick, J. (1985). Negative staining of myosin molecules. J. Mol. Biol. 184, 535-542.
42. Walzthöny D., Bähler, M., Eppenberger, H. M., Wallimann, T. & Engel, A. (1984). Unshadowed myosin molecules: STEM mass-maps of myosin heads. EMBO J. 3, 2621-2626.
43. Ward, R. (1985). The properties of myosin rod and the structure of the vertebrate striated thick filament. PhD thesis, University of London.
44. Xie, X., Harrison, D. H., Schlichting, I., Sweet, R. M., Kalabokis, V. N., Szent-Györgyi, A. G. & Cohen, C. (1994). Structure of the regulatory domain of scallop myosin at 2.8 Å resolution. Nature, 368, 306-312.