Cloning, nucleotide sequence and characterization of a full-length cDNA encoding the myosin heavy chain from adult chicken pectoralis major muscle

Gene

Volumn 199, Issue 1-2, 1997, Pages 265-270

  Chao, Ta Hsiang ^a   Bandman, Everett ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Baculovirus; Sf9 insect cell

Indexed keywords

COMPLEMENTARY DNA; MONOCLONAL ANTIBODY; MYOSIN HEAVY CHAIN;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; BACULOVIRUS; CELL LINE; CHICKEN; DNA LIBRARY; DNA PROBE; HYDROPHILICITY; INSECT; ISOELECTRIC POINT; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PECTORALIS MAJOR MUSCLE; PRIORITY JOURNAL; PROTEIN ANALYSIS; VIRUS RECOMBINANT;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; ANTIBODIES, MONOCLONAL; BACULOVIRIDAE; BASE SEQUENCE; CELL LINE; CHICKENS; CLONING, MOLECULAR; DNA, COMPLEMENTARY; GENETIC VECTORS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MYOSIN HEAVY CHAINS; PECTORALIS MUSCLES; RECOMBINANT FUSION PROTEINS; SARCOMERES; SEQUENCE ANALYSIS, DNA; SPODOPTERA;

EID: 0030866054     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00386-7     Document Type: Article

References (37)

1. Adelstein, R.S., Eisenberg, E., 1980. Regulation and kinetics of the actin-myosin-ATP interaction. Ann. Rev. Biochem. 49, 921-956.
2. Bandman, E., 1985. Continued expression of neonatal myosin heavy chain in adult dystrophic skeletal muscle. Science 227, 780-782.
3. Bandman, E., Bennett, T., 1988. Diversity of fast myosin heavy chain expression during development of gastrocnemius, bicep brachii, and posterior latissimus dorsi muscle in normal and dystrophic chicken. Dev. Biol. 130, 220-231.
4. Biro, N.A., Szilagyi, L., Balint, M., 1972. Studies on the helical segment of the myosin molecule. Cold Spring Harbor Symp. Quant. Biol. 37, 55-63.
5. Cerny, L.C., Bandman, E., 1987. Expression of myosin heavy chain isoforms in regenerating myotubes of innervated and denervated chicken muscle. Dev. Biol. 119, 350-362.
6. Davis, J.S., 1988. Assembly processes in vertebrate skeletal thick filament formation. Ann. Rev. Biophys. Chem. 17, 217-239.
7. Emerson, C.P., Bernstein, S.I., 1987. Molecular genetics of myosin. Ann. Rev. Biochem. 56, 695-726.
8. Gazith, J., Himmelfarb, S., Harrington, W.F., 1970. Studies on the subunit structure of myosin. J. Biol. Chem. 245, 15-22.
9. Gershman, L.C., Stratcher, A., Dreizen, P., 1969. Subunit structure of myosin. III. A proposed model for rabbit skeletal myosin. J. Mol. Biol. 224, 2726-2736.
10. Harrington, W.F., Burke, M., Barton, J.S., 1972. Contraction of myofibrils in the presence of antibodies to myosin subfragment 2. Cold Spring Harbor Symp. Quant. Biol. 37, 64-85.
11. Hopp, T.P., Woods, K.R., 1981. Prediction of protein antigenic determinants from amino acid sequences. Proc. Natl. Acad. Sci. USA 78, 3824-3828.
12. Kinose, F., Wang, S.X., Kidambi, U.S., Moncman, C.L., Winkelmann, D.A., 1996. Glycine 699 is pivotal for the motor activity of skeletal muscle myosin. J. Cell Biol. 134, 895-909.
13. Korn, E.D., Hammer, J.A., 1988. Myosin of nonmuscle cells. Ann. Rev. Biophys. Chem. 17, 23-45.
14. Kropp, K., Gulick, J., Robbins, J., 1986. A canonical sequence organization at the 5′-end of the myosin heavy chain genes. J. Biol. Chem. 261, 6613-6618.
15. Laemmli, U.K., 1970. Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
16. Lowey, S., Risby, D., 1971. Light chains from fast and slow muscle myosins. Nature 234, 81-85.
17. Lowey, S., Slayter, H.S., Weeds, A.G., Baker, H., 1969. Substructure of the myosin molecule. I. Subfragments of myosin by enzymatic degradation. J. Mol. Biol. 42, 1-29.
18. Lowey, S., Waller, G.S., Bandman, E., 1991. Neonatal and adult myosin heavy chains form homodimers during avian skeletal development. J. Cell Biol. 113, 303-310.
19. McNally, E., Sohn, R., Frankel, S., Leinwand, L., 1991. Expression of myosin and actin in Escherichia coli. Meths Enzymol. 196, 368-389.
20. Maita, T., Yajima, E., Nagata, S., Miyanishi, T., Nakayama, S., Matsuda, G., 1991. The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1938-residue sequence of the heavy chain. J. Biochem. (Tokyo) 110, 75-87.
21. Miller, J.B., Teal, S.B., Stockdale, F.E., 1989. Evolutionarily conserved sequences of striated muscle myosin heavy chain isoforms. J. Biol. Chem. 264, 13122-13130.
22. Molina, M.I., Kropp, K.E., Gulick, J., Robbins, J., 1987. The sequence of an embryonic myosin heavy chain gene and isolation of its corresponding cDNA. J. Biol. chem. 262, 6478-6488.
23. Moore, L.A., Arrizubieta, M.J., Tidyman, W.T., Herman, L.A., Bandman, E., 1992. Analysis of the chicken fast myosin heavy chain gene family: Localization of isoform-specific antibody epitopes and regions of divergence. J. Mol. Biol. 223, 383-387.
24. Mueller, H., Perry, S.V., 1962. The degradation of heavy meromyosin by trypsin. Biochem. J. 85, 431-439.
25. O'Reilly, D.R., Miller, L.K., Luckow, V.A., 1992. Baculovirus Expression Vector: A Laboratory Manual. Freeman and Co., New York.
26. Pato, M.D., Seller, J.R., Preston, Y.A., Harvey, E.V., Adelstein, R.S., 1996. Baculovirus expression of chicken nonmuscle heavy meromyosin II-B. J. Biol. Chem. 271, 2689-2695.
27. Pepe, F.A., 1967. The myosin filament. I. Structural organization from antibody staining observed in electron microscopy. J. Mol. Biol. 27, 203-225.
28. Rayment, I., Rypnicwski, W.R., Schmidt-Base, K., Smith, R., Tomchick, D.R., Benning, M.M., Winkelmann, D.A., Wesenberg, G., Holden, H.M., 1993a. The three dimensional structure of a molecular motor, myosin subfragment-1. Science 261, 50-58.
29. Rayment, I., Holden, H.M., Whittker, 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.
30. Sambrook, J., Fritsch, E.F., Maniatis, T., 1989. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
31. Sweeney, H.L., Straceski, A., Leinwand, L.A., Tikunov, B.A., Faus, L., 1994. Heterologous expression of a cardiomyopathic myosin that is defective in its actin interaction. J. Biol. Chem. 269, 1603-1605.
32. Tan, J.L., Ravid, S., Spudich, J.A., 1992. Control of nonmuscle myosins by phosphorylation. Ann. Rev. Biochem. 61, 721-759.
33. Thomas, D.D., Seidel, J.C., Hyde, J.S., Gergely, J., 1975. Motion of subfragment-1 in myosin and its supramolecular complexes: Saturation transfer electron paramagnetic resonance. Proc. Natl. Acad. Sci. USA 72, 1729-1733.
34. Trybus, K.M., 1994. Regulation of expressed truncated smooth muscle myosins: Role of the essential light chain and tail length. J. Biol. Chem. 269, 20819-20822.
35. Warrick, H.M., Spudich, J.A., 1987. Myosin structure and function in cell motility. Ann. Rev. Cell Biol. 3, 379-421.
36. Weeds, A., Pope, B.J., 1977. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111, 129-157.
37. Winkelmann, D.A., Lowey, S., Press, J.L., 1983. Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis. Cell 34, 295-306.