Correlation between Mechanical and Enzymatic Events in Contracting Skeletal Muscle Fiber

Biochemistry

Volumn 43, Issue 10, 2004, Pages 2804-2811

  Shepard, A ^a   Borejdo, J ^a  

^a UNIVERSITY OF NORTH TEXAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; DESORPTION; DISSOCIATION; ENZYME KINETICS; FLUORESCENCE; HYDROLYSIS; MUSCLE;

MYOSIN;

BIOCHEMISTRY;

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GLYCEROL; MYOSIN; MYOSIN SUBFRAGMENT;

ACTIN MYOSIN INTERACTION; ANIMAL TISSUE; ARTICLE; BIOMECHANICS; DESORPTION; DISSOCIATION; ENZYME MECHANISM; FLUORESCENCE; HYDROLYSIS; MECHANICAL PROBE; MUSCLE CONTRACTION; MUSCLE FIBER CROSS BRIDGE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PSOAS MUSCLE; RABBIT; SKELETAL MUSCLE; THIN FILAMENT;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; BIOMECHANICS; FLUORESCENCE POLARIZATION; KINETICS; MUSCLE CONTRACTION; MUSCLE FIBERS; MYOSIN LIGHT CHAINS; MYOSINS; PSOAS MUSCLES; RABBITS; RHODAMINES;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 1542267782     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030233d     Document Type: Article

References (37)

1. Saito, K., Aoki, T., and Yanagida, T. (1994) Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap, Biophys. J. 66, 769-777.
2. Yanagida, T., Kitamura, K., Tanaka, H., Hikikoshi Iwane, A., and Esaki, S. (2000) Single molecule analysis of the actomyosin motor, Curr. Opin. Cell Biol. 12, 20-25.
3. Ishijima, A., Kojima, H., Funatsu, T., Tokunaga, M., Higuchi, H., Tanaka, H., and Yanagida, T. (1998) Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin, Cell 92, 161-171.
4. Funatsu, T., Harada, Y., Tokunaga, M., Saito, K., and Yanagida, T. (1995) Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution, Nature 374, 555-559.
5. Warshaw, D. M., Hayes, E., Gaffney, D., Lauzon, A. M., Wu, J., Kennedy, G., Trybus, K., Lowey, S., and Berger, C. (1998) Myosin conformational states determined by single fluorophore polarization, Proc. Natl. Acad. Sci. U.S.A. 95, 8034-8039.
6. Minton, A. P. (1998) Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion, Methods Enzymol. 295, 127-149.
7. Arakawa, T., and Timasheff, S. N. (1985) Theory of protein solubility, Methods Enzymol. 114, 49-77.
8. Andreev, O. A., and Borejdo, J. (1991) Myosin head can bind two actin monomers, Biochem. Biophys. Res. Commun. 177, 350-356.
9. Andreev, O. A., Andreeva, A. L., Markin, V. S., and Borejdo, J. (1993) Two different rigor complexes of myosin subfragment-1 and actin, Biochemistry 32, 12046-12035.
10. Borejdo, J., and Akopova, I. (2003) Orientational changes of cross-bridges during single turnover of ATP, Biophys. J. 84, 2450-2459.
11. Dos Remedios, C. G., Millikan, R. G., and Morales, M. F. (1972) Polarization of tryptophan fluorescence from single striated muscle fibers. A molecular probe of contractile state, J. Gen. Physiol. 59, 103-120.
12. Cooke, R., Crowder, M. S., and Thomas, D. D. (1982) Orientation of spin labels attached to cross-bridges in contracting muscle fibres, Nature 300, 776-778.
13. Burghardt, T. P., Garamszegi, S. P., Park, S., and Ajtai, K. (1998) Tertiary structural changes in the cleft containing the ATP sensitive tryptophan and reactive thiol are consistent with pivoting of the myosin heavy chain at Gly699, Biochemistry 37, 8035-8047.
14. Highsmith, S., and Eden, D. (1993) Myosin-ATP chemomechanics, Biochemistry 32, 2455-2458.
15. Rayment, I., Rypniewski, W., Schmidt-Base, K., Smith, R., Tomchik, D. R., Benning, M. M., Winkelman, D. A., Wesenberg, G., and Holden, H. M. (1993) Three-dimensional structure of myosin subfragment-1: a molecular motor, Science 261, 50-58.
16. Cooke, R. (1997) Actomyosin interaction in striated muscle, Physiol. Rev. 77, 671-697.
17. Goldman, Y. E. (1998) Wag the tail: structural dynamics of actomyosin, Cell 93, 1-4.
18. Dominguez, R., Freyzon, Y., Trybus, K. M., and Cohen, C. (1998) Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state, Cell 94, 559-571.
19. Houdusse, A., Kalabokis, V. N., Himmel, D., Szent-Gyorgyi, A. G., and Cohen, C. (1999) Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head, Cell 97, 459-470.
20. Warshaw, D. M., Guilford, W. H., Freyzon, Y., Krementsova, E., Palmiter, K. A., Tyska, M. J., Baker, J. E., and Trybus, K. M. (2000) The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever, J. Biol. Chem. 275, 37167-37172.
21. Allen, T. S.-C., Ling, N., Irving, M., and Goldman, Y. E. (1996) Orientation changes in myosin regulatory light chains following photorelease of ATP in skinned muscle fibers, Biophys. J. 70, 1847-1862.
22. Borejdo, J., Ushakov, D. S., and Akopova, I. (2002) The regulatory and essential light chains of myosin rotate equally during contraction of skeletal muscle, Biophys. J. 82, 3150-3159.
23. Pesce, A. J., Rosen, C.-G., and Pasby, T. L. (1971) in Fluorescence Spectroscopy, Marcel Dekker, New York.
24. Highsmith, S., Mendelson, R. A., and Morales, M. F. (1976) Affinity of myosin S-1 for F-actin, measured by time-resolved fluorescence anisotropy, Proc. Natl. Acad. Sci. U.S.A. 73, 133-137.
25. Weiss, S., Rossi, R., Pellegrino, M. A., Bottinelli, R., and Geeves, M. A. (2001) Differing ADP release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers, J. Biol. Chem. 276, 45902-45908.
26. Chaen, S., Shirakawa, I., Bagshaw, C. R., and Sugi, H. (1997) Measurement of nucleotide release kinetics in single skeletal muscle myofibrils during isometric and isovelocity contractions using fluorescence microscopy, Biophys. J. 73, 2033-2042.
27. Shirakawa, I., Chaen, S., Bagshaw, C. R., and Sugi, H. (2000) Measurement of nucleotide exchange rate constants in single rabbit soleus myofibrils during shortening and lengthening using a fluorescent ATP analogue, Biophys. J. 78, 918-926.
28. Tonomura, Y., Appel, P., and Morales, M. F. (1966) On the molecular weight of myosin. II, Biochemistry 5, 515-521.
29. Sabido-David, C., Hopkins, S. C., Saraswat, L. D., Lowey, S., Goldman, Y. E., and Irving, M. (1998) Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibres, J. Mol. Biol. 279, 387-402.
30. Wolff-Long, V. L., Saraswat, L. D., and Lowey, S. (1993) Cysteine mutants of light chain-2 form disulfide bonds in skeletal muscle myosin, J. Biol. Chem. 268, 23162-23167.
31. Ling, N., Shrimpton, C., Sleep, J., Kendrick-Jones, J., and Irving, M. (1996) Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle, Biophys. J. 70, 1836-1846.
32. Sabido-David, C., Brandmeier, B., Craik, J. S., Corrie, J. E., Trentham, D. R., and Irving, M. (1998) Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethylrhodamine, Biophys. J. 74, 3083-3092.
33. Burghardt, T. P., Cruz-Walker, A. R., Park, S., and Ajtai, K. (2001) Conformation of Myosin Interdomain Interactions During Contraction: Deductions from muscle fibers using polarized fluorescence, Biochemistry 40, 4821-4833.
34. Oiwa, K., Jameson, D. M., Croney, J. C., Davis, C. T., Eccleston, J. F., and Anson, M. (2003) The 2′-O- and 3′-O-Cy3-EDA-ATP-(ADP) complexes with myosin subfragment-1 are spectroscopically distinct, Biophys. J. 84, 634-642.
35. Hubley, M. J., Locke, B. R., and Moerland, T. S. (1996) The effects of temperature, pH, and magnesium on the diffusion coefficient of ATP in solutions of physiological ionic strength, Biochim. Biophys. Acta 1291, 115-121.
36. Ajtai, K., Ilich, P. J., Ringler, A., Sedarous, S. S., Toft, D. J., and Burghardt, T. P. (1992) Stereospecific reaction of muscle fiber proteins with the 5′ or 6′ isomer of (iodoacetamido)tetramethyl-rhodamine, Biochemistry 31, 12431-12440.
37. Lymn, R. W., and Taylor, E. W. (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin, Biochemistry 10, 4617-4624.