Characterization of the interaction of myosin with ATP analogues having the syn conformation with respect to the adenine-ribose bond

European Journal of Biochemistry

Volumn 256, Issue 1, 1998, Pages 229-237

  Maruta, Shinsaku ^a   Ohki, Takashi ^a   Kambara, Taketoshi ^b   Ikebe, Mitsuo ^b  

^a SOKA UNIVERSITY   (Japan)

^b UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

ATP analogue; ATPase site; Muscle contraction; Myosin; Photoaffinity labeling

Indexed keywords

ADENINE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE DERIVATIVE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; RIBOSE;

ANIMAL TISSUE; ARTICLE; BINDING SITE; CHICKEN; MUSCLE; MUSCLE CONTRACTION; NONHUMAN; PHOTOAFFINITY LABELING; PRIORITY JOURNAL;

ANIMALIA; GALLUS GALLUS;

EID: 0032528833     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2560229.x     Document Type: Article

References (45)

1. Hartshorne, D. J. (1987) in Physiology of the gastrointestinal tract (Johnson, L. R., ed.) 2nd edn, vol. 1, pp. 423-482, Raven, New York.
2. Mooseker, M. S. & Chenney, R. E. (1995) Unconventional myosins, Annu. Rev. Cell Rev. Biol. 11, 633-675.
3. Tan, J. L., Ravid, S. & Spudich, J. A. (1992) Control of nonmuscle myosins by phosphorylation, Annu. Rev. Biochem. 61, 721-759.
4. Van Buren, P., Work, S. & Warshaw, D. M. (1994) Enhanced force generation by smooth muscle myosin in vitro, Proc. Natl Acad. Sci. USA 91, 202-205.
5. Kamm, K. E. & Stull, J. T. (1989) Regulation of smooth muscle contractile elements by second messengers, Annu. Rev. Physiol. 52, 299-313.
6. Sellers, J. R. & Adelstein, R. S. (1987) in The enzymes (Boyer, P. & Krebs, E. G., eds) vol. 18, pp. 381-418, Academic Press, San Diego.
7. Rayment, I., Holden, H. M., Whittacker, M., Yohn, C. B., Lorenzs, M., Holmes, K. C. & Milligand, R. A. (1993) Three-dimensional structure of myosin subfragment-1; a molecular motor, Science 261, 50-58.
8. Spudich, J. A. (1994) How molecular motors work, Nature 372, 515-518.
9. Cole, D. G. & Yount, R. G. (1990) Photolabeling of the 6 and 10 S conformations of gizzard myosin with 3′(2′)-O-(4-Benzoyl)benzoyl-ATP. Proline 324 is near the active site, J. Biol. Chem. 265, 22537-22546.
10. 3H]uridine diphosphate places Glu 185 of the heavy chain at the active site, J. Biol. Chem. 265, 22547-22553.
11. Chabre, M. (1990) Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology, Trends Biochem. Sci. 15, 6-10.
12. Goodno, C. C. (1979) Inhibition of myosin ATPase by vanadate ion, Proc. Natl Acad. Sci. USA 76, 2620-2624.
13. Goodno, C. C. & Taylor, E. R. W. (1982) Inhibition of actomyosin ATPase by vanadate, Proc. Natl Acad. Sci. USA 79, 21-25.
14. 19F-NMR, Biophys. J. 59, 436a.
15. 19F-NMR, J. Biol. Chem. 268, 7093-7100.
16. Maruta, S., Henry, G. D., Sykes, B. D. & Ikebe, M. (1993b) Myosin-ADP-fluoroaluminate and myosin-ADP-fluoroberyllate ternary complexes as transition state analogues, Biophys. J. 64, 141a.
17. Phan, B. & Reisler, E. (1992) Inhibition of myosin ATPase by beryllium fluoride, Biochemistry 31, 4787-4793.
18. Weber, M., Peyser, Y. M. & Muhlrad, A. (1992) Characterization of stable beryllium fluoride, aluminum fluoride, and vanadate containing myosin subfragment 1-nucleotide complexes, Biochemistry 31, 7190-7197.
19. 4, Biochemistry 34, 8960-8972.
20. Smith, A. J. & Rayment, I. (1996) X-ray structure of the magnesium(II). ADP · vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution, Biochemistry 35, 5404-5417.
21. Takenaka, H., Ikehara, M. & Tonomura, Y. (1976) Structure and function of the two heads of the myosin molecule. IV. Physiological functions of various reaction intermediates in myosin adenosine triphosphatase, studied by the interaction between actomyosin and 8-bromoadenosine triphosphate, J. Biochem. (Tokyo) 80, 1381-1392.
22. Takenaka, T., Ikehara, M. & Tonomura, Y. (1978) Interaction between actomyosin and 8-substituted ATP analogs, Proc. Natl Acad. Sci. USA 75, 4229-4233.
23. Miles, D. W., Townsend, L. B., Robins, M. J., Inskeep, W. H. & Eyring, H. (1971) Circular dichroism of nucleoside derivatives. X. Influence of solvents and substituents upon the Cotton effects of guanosine derivatives, J. Am. Chem. Soc. 93, 1600-1608.
24. Uesugi, S. & Ikehara, M. (1977) Carbon-13 Magnetic resonance spectra of 8-substituted purine nucleotides. Characteristic shifts for the syn conformation, J. Am. Chem. Soc. 99, 3250-3253.
25. 1-ATPase, FEBS Lett. 242, 178-182.
26. 31P) fast Fourier transform nuclear magnetic resonance methods and conformational energy calculations, J. Am. Chem. Soc. 96, 7337-7348.
27. Perry, S. V. (1952) Myosin adenosine triphosphatase, Methods Enzymol. 2, 582-588.
28. Weeds, A. G. & Taylor, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin, Nature 25, 54-56.
29. 2+ on the conformation and enzymatic activity of smooth muscle myosin, J. Biol. Chem. 260, 13146-13153.
30. Ikebe, M., Stepinska, M., Kemp, B. E., Means, A. R. & Hartshorne, D. J. (1987) Proteolysis of smooth muscle myosin light chain kinase. Formation of inactive and calmodulin-independent fragments, J. Biol. Chem. 262, 13828-13834.
31. Walsh, M. P., Hinkins, S., Dabrowska, R. & Hartshorne, D. J. (1983) Smooth muscle myosin light chain kinase, Methods Enzymol. 99, 279-288.
32. Maruta, S., Miyanishi, T. & Matsuda, G. (1989) Localization of the ATP-binding site in the 23-kDa and 20-kDa regions of the heavy chain of the skeletal muscle myosin head, Eur. J. Biochem. 184, 213-221.
33. Youngburg, G. E. & Youngburg, M. V. (1930) A system of blood phosphorus analysis, J. Lab. Clin. Med. 16, 158-166.
34. Sata, M., Matsuura, M. & Ikebe, M. (1996) Characterization of the motor and enzymatic properties of smooth muscle long S1 and short HMM: role of the two-headed structure on the activity and regulation of the myosin motor, Biochemistry 35, 11113-11118.
35. Penefsky, H. S. (1977) Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase, J. Biol. Chem. 252, 2891-2899.
36. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
37. Hiratsuka, T. (1993) Behavior of Cys-707 (SH1) in myosin associated with ATP hydrolysis revealed with a fluorescent probe linked directly to the sulfur atom, J. Biol. Chem. 268, 24742-24750.
38. Fujii, S., Fujiwara, T. & Tomita, K. (1976) Structural studies on the two forms of 8-bromo-2′,3′-O-isopropylideneadenosine, Nucleic Acids Res. 3, 1985-1996.
39. Tavale, S. S. & Sobell, X. X. (1970) Crystal and molecular structure of 8-bromoguanosine and 8-bromoadenosine, two purine nucleosides in the syn conformation, J. Mol. Biol. 48, 109-123.
40. Wang, D., Pate, E., Cooke, R. & Yount, R. (1993) Synthesis of non-nucleotide ATP analogues and characterization of their chemomechanical interaction with muscle fibres, J. Muscle Res. Cell Motil. 14, 484-497.
41. Grammer, J. C., Kuwayama, H. & Yount, R. G. (1993) Photoaffinity labeling of skeletal myosin with 2-azidoadenosine triphosphate, Biochemistry 32, 5725-5732.
42. Mahmood, R., Elzinga, M. & Yount, R. G. (1989) Serine-324 of myosin's heavy chain is photoaffinity-labeled by 3′(2′)-O-(4-benzoylbenzoyl)adenosine triphosphate, Biochemistry 28, 3989-3995.
43. Abdallah, M. A., Beillmann, J. F., Nordstrom, B. & Branden, C. I. (1975) The conformation of adenosine diphosphoribose and 8-bromoadenosine diphosphoribose when bound to liver alcohol dehydrogenase, Eur. J. Biochem. 50, 475-481.
44. Maita, T., Hayashida, M., Tanioka, Y. Komine, Y. & Matsuda, G. (1987) The primary structure of the myosin head, Proc. Natl Acad. Sci. USA 84, 416-420.
45. Yanagisawa, M., Hamada, Y. Katsuragawa, Y., Imamura, M., Mikawa, T. Masaki, T. (1987) Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin, J. Mol. Biol. 198, 143-157.