Filament assembly properties of the sarcomeric myosin heavy chain

Poultry Science

Volumn 78, Issue 5, 1999, Pages 735-742

  Wick, Macdonald ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

Assembly; Myosin; Parallel dimer; Sarcomere; Synthetic filament

Indexed keywords

ANIMALIA;

MYOSIN HEAVY CHAIN;

ANIMAL; ARTICLE; CHEMISTRY; MEAT; METABOLISM; MUSCLE CELL; PHYSIOLOGY; POULTRY; SARCOMERE; SKELETAL MUSCLE; ULTRASTRUCTURE;

ANIMALS; MEAT; MUSCLE FIBERS; MUSCLE, SKELETAL; MYOSIN HEAVY CHAINS; POULTRY; SARCOMERES;

EID: 0033129060     PISSN: 00325791     EISSN: None     Source Type: Journal    
DOI: 10.1093/ps/78.5.735     Document Type: Article

References (56)

1. Atkinson, S. J., and M. Stewart, 1991a. Expression in Escherichia coli of fragments of the coiled-coil rod domain of rabbit myosin: influence of different regions of the molecule on aggregation and paracrystal formation. J. Cell Sci. 99: 823-836.
2. Atkinson, S. J., and M. Stewart, 1991b. Molecular basis of myosin assembly: coiled-coil interactions and the role of charge periodicities. J. Cell Sci. 14:7-10.
3. Atkinson, S. J., and M. Stewart, 1992. Molecular interactions in myosin assembly role of the 28-residue repeat in the rod. J. Mol. Biol. 226:7-13.
4. Baba, M. L., M. Goodman, J. Berger-Cohn, J. G. Demaille, and G. Matsuda, 1984. The early adaptive evolution of calmodulin. Mol. Biol. Evol. 1:442-455.
5. Bandman, E., L. A. Moore, M. J. Arrizubieta, W. E. Tidyman, L. Herman and M. Wick, 1994. The evolution of the chicken sarcomeric myosin heavy chain multigene family. Pages 129-139 in: Proceedings of Society of General Physiologists 47th Annual Symposium. The Rockefeller University Press, New York, NY.
6. Cheney, R. E., M. A. Riley, and M. S. Mooseker, 1993. Phylogenetic analysis of the myosin superfamily. Cell Motil. Cytoskel. 24:215-223.
7. Chowrashi, P. K., S. M. Pemrick, and F. A. Pepe, 1989. LC2 involvement in the assembly of skeletal myosin filaments. Biochim. Biophys. Acta 990:216-223.
8. Chowrashi, P. K., and F. A. Pepe, 1977. Light meromyosin paracrystal formation. J. Cell Biol. 74:136-152.
9. Cohen, C., and D.A.D. Parry, 1986. Alpha helical coiled coils - a wide spread motif in proteins. Trends Biochem. Sci. 11: 245-248.
10. Cohen, C., and D.A.D. Parry, 1990. Alpha-helical coiled coils and bundles: how to design an alpha-helical protein. Proteins 7:1-15.
11. Collins, J., 1976. Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbumin. Nature 259:699-700.
12. Crick, F.H.C., 1953. The packing of a-helices: simple coiled-coils. Acta Cryst. 6:689-697.
13. Davis, J. S., 1985. Kinetics and thermodynamics of the assembly of the parallel- and antiparallel-packed sections of synthetic thick filaments of skeletal myosin: a pressure-jump study. Biochemistry 24:5263-5269.
14. Davis, J. S., 1986. A model for length-regulation in thick filaments of vertebrate skeletal myosin. Biophys J. 50: 417-422.
15. Davis, J. S., 1988a. Assembly process in vertebrate skeletal thick filament formation. Ann. Rev. Biophys. Biophys. Chem. 17:217-239.
16. Davis, J. S., 1988b. Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle. J. Mus. Res. Cell Motil. 9: 174-183.
17. Davis, J. S., J. Buck, and E. P. Greene, 1982. The myosin dimer: an intermediate in the self-assembly of the thick filament of vertebrate skeletal muscle. FEBS Lett. 140:293-297.
18. Goodson, H. V., and J. A. Spudich, 1993. Molecular evolution of the myosin family: Relationships derived from comparisons of amino acid sequences. Proc. Nat. Acad. Sci. USA 90:659-663.
19. Harrison, R. G., S. Lowey, and C. Cohen, 1971. Assembly of myosin. J. Mol. Biol. 59:531-535.
20. Hickmand, C. L., 1970. Integrated Principles of Zoology. 4th rev. ed. The C. V. Mosby Co., Saint Louis, MO.
21. Huxley, H. E., 1963. Electron microscope studies on the structure of natural and synthetic filaments from striated muscle. J. Mol. Biol. 7:281-308.
22. Josephs, R., and W. F. Harrington, 1966. Studies on the formation and physical chemical properties of synthetic myosin filaments. Biochemistry 11:3474-3487.
23. Katsura, I., and H. Noda, 1971. Studies on the formation and physical chemical properties of synthetic myosin filaments. J. Biochem. 69:219-229.
24. Lee, R. J., T. T. Egelhoff, and J. A. Spudich, 1994. Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain. J. Cell Sci. 102:2875-2886.
25. Letai, A., and E. Fuchs, 1995. The importance of intramolecular ion pairing in intermediate filaments. Biochemistry 92: 92-96.
26. Lowey, S., and D. Risby, 1971. Light chains from fast and slow muscle myosins. Nature 234:81-85.
27. Margossian, S. S., A. K. Bhan, and H. S. Slayter, 1983. Role of the regulatory light chains in skeletal muscle actomyosin ATPase and in minifilament formation. J. Biol. Chem. 258: 13359-13369.
28. McLachlan, A. D., and J. Karn, 1982. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature 299: 226-231.
29. McLachlan, A. D., and M. Stewart, 1975. Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure. J. Mol. Biol. 98:293-304.
30. McNally, E. M., R. Kraft, M. Bravo-Zehnder, D. A. Taylor, and L. A. Leinwand, 1989. Full-length rat alpha and beta cardiac myosin heavy chain sequences. Comparisons suggest a molecular basis for functional differences. J. Mol. Biol. 210:665-671.
31. Mihalyi, E., and A. G. Szent-Gyorgyi, 1953. Trypsin digestion of muscle proteins. I. Ultracentrifugal analysis of the process. J. Biol. Chem. 201:189-196.
32. Moos, R. L., G. M. Diffee, and M. L. Greaser, 1995. Contractile properties of skeletal muscle fibers in relation to myofibrillar protein isoforms. Rev. Physiol. Biochem. Pharmacol. 126:1-63.
33. Nguyen, H. T., R. M. Gubits, R. M. Wydro, and B. Nadal-Ginard, 1982. Sarcomeric myosin heavy chain is coded by a highly conserved multigene family. Proc. Nat. Acad. Sci. USA 79:5230-5234.
34. O'Halloran, T. J., S. Ravid, and J. A. Spudich, 1990. Expression of Dictyostelium myosin tail segments in Escherichia coli: Domains required for assembly and phosphorylation. J. Cell Biol. 110:63-70.
35. Parry, D. A., 1981. Structure of rabbit skeletal myosin. Analysis of the amino acid sequences of two fragments from the rod region. J. Mol. Biol. 153:459-464.
36. Pinset-Harstrom, I., and J. Truffy, 1979. Effect of adenosine triphosphate, inorganic phosphate and divalent cations on the size and structure of synthetic myosin filaments. J. Mol. Biol. 134:173-188.
37. Pollard, T. D., 1975. Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge flexibility and copolymer formation. J. Cell Biol. 67:93-104.
38. Reisler, E., P. Cheung, and N. Borochov, 1986a. Macromolecular assemblies of myosin. Biophys J. 49:335-342.
39. Reisler, E., P. Cheung, N. Borochov, and J. A. Lake, 1986b. Monomers, dimers, and minifilaments of vertebrate skeletal myosin in the presence of sodium pyrophosphate. J. Biochem. 25:326-332.
40. Reisler, E., P. Cheung, C. Oriol-Audit, and J. A. Lake, 1982. Growth of synthetic myosin filaments from myosin minifilaments. Biochemistry 21:701-707.
41. Rice, R. V., 1961. Conformation of individual macromolecular particles from myosin solutions. Biochim. Biophys. Acta 52:602-604.
42. Rosser, B.W.C., and J. C. George, 1986a. The avian pectoralis: histochemical characterization and distribution of muscle fiber types. Can. J. Zool. 64:1174-1185.
43. Rosser, B.W.C., and J. C. George, 1986b. Slow muscle fibers in the pectoralis of the turkey vulture (Cathartes aura): an adaptation for soaring flight. Zool. Anz. 217:252-258.
44. Seiler, S. H., D. A. Fischman, and L. A. Leinwand, 1996. Modulation of myosin filament organization by C-protein family members. Mol. Biol. Cell 7:113-127.
45. 2- and COOH-terminal deletions. J. Cell Biol. 111:2417-2426.
46. Sinard, J. H., W. F. Stafford, and T. D. Pollard , 1989. The mechanism of assembly by three successive dimerization steps. J. Cell Biol. 109:1537-1547.
47. Sjostrom, M., and J. M. Squire, 1977. Fine structure of the A-band in cryo-sections: The structure of the A-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained. J. Mol. Biol. 109:49-68.
48. Squire, J. M., and P. J. Vilbert, 1987. Pages 247-281 in: Fibrous Protein Structure. Academic Press, London, U.K.
49. Strehler, E. E., M.-A. Strehler-Page, J.-C. Perriard, M. Periasamy, and B. Nadal-Ginard, 1986. Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain gene: Evidence against intron-dependent evolution of the rod. J. Mol. Biol. 190:291-317.
50. Strzelecka-Golaszewska, H., L. Nyitray, and M. Balint, 1985. Paracrystalline assemblies of light meromyosins with various chain weights. J. Mus. Res. Cell Motil. 6:641-658.
51. Tan, J. L., S. Ravid, and J. A. Spudich, 1992. Control of nonmuscle myosins by phosphorylation. Ann. Rev. Biochem:721-759.
52. Trybus, K. M., 1989. Filamentous smooth muscle myosin is regulated by phosphorylation. J. Cell Sci. 109:2887-2894.
53. Ward, R., and P. Bennett, 1989. Paracrystals of myosin rod. J. Muscle Res. Cell Motil. 10:34-52.
54. Wick, M., F. Tablin, and E. Bandman, 1997. Effects of anti-LMM antibodies on the solubility of chicken skeletal muscle myosin. J. Food Biochem. 20:379-395.
55. Xiong, Y. L., 1992. Thermally induced interactions and gelation of combined myofibrillar protein from white and red broiler muscles. J. Food Sci. 577:582-585.
56. Xiong, Y. L., 1994. Myofibrillar protein from different muscle fiber types: Implications of biochemical and functional properties in meat processing. Crit. Rev. Food Sci. Nutr. 34:293-320.