Structural changes of actin-bound myosin heads after a quick length change in frog skeletal muscle

Biophysical Journal

Volumn 89, Issue 2, 2005, Pages 1150-1164

  Yagi, Naoto ^a   Iwamoto, Hiroyuki ^a   Wakayama, Jun'ichi ^a   Inoue, Katsuaki ^a  

^a JAPAN SYNCHROTRON RADIATION RESEARCH INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MUSCLE PROTEIN; MYOSIN;

ANIMAL EXPERIMENT; ARTICLE; FROG; MUSCLE CONTRACTION; MUSCLE LENGTH; MUSCLE STRETCHING; MUSCLE TONE; NONHUMAN; PROTEIN STRUCTURE; SARTORIUS MUSCLE; SKELETAL MUSCLE; X RAY DIFFRACTION;

ANURA;

EID: 23244433044     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.059089     Document Type: Article

References (33)

1. Elliott, G. F., J. Lowy, and B. M. Millman. 1967. Low-angle x-ray diffraction studies of living striated muscle during contraction. J. Mol. Biol. 25:31-45.
2. Huxley, H. E., and W. Brown. 1967. The low-angle x-ray diagram of vertebrate striated muscle and its behavior during contraction and rigor. J. Mol. Biol. 30:383-434.
3. Huxley, H. E., A. R. Faruqi, J. Bordas, M. H. J. Koch, and J. R. Milch. 1980. The use of synchrotron radiation in time-resolved x-ray diffraction studies of myosin layer-line reflections during muscle contraction. Nature. 284:140-143.
4. Huxley, H. E., R. M. Simmons, A. R. Faruqi, M. Kress, J. Bordas, and M. H. J. Koch. 1983. Changes in the x-ray reflections from contracting muscle during rapid mechanical transients and their structural implications. J. Mol. Biol. 168:469-506.
5. Irving, M., V. Lombardi, G. Piazzessi, and M. A. Ferenczi, 1992. Myosin head movements are synchronous with the elementary force-generating process in muscle. Nature. 357:156-158.
6. Bordas, J., G. P, Diakun, F. G. Diaz, J. E. Harries, R. A. Lewis, J. Lowy, G. R. Mant, L. Martin-Fernandez, and E. Towns-Andrews. 1993. Two-dimensional time-resolved x-ray diffraction studies of live isometrically contracting frog sartorius muscle. J. Muscle Res. Cell Motil. 14:311-324.
7. Bordas, J., A. Svensson, M. Rothery, J. Lowy, G. P. Diakun, and P. Boesecke. 1999. Extensibility and symmetry of actin filaments in contracting muscles. Biophys. J. 77:3197-3207.
8. Irving, M., G. Piazzessi, L. Lucii, Y.-U. Sun, J. J. Harford, I. M. Dobbie, M. A. Ferenczi, M. Reconditi, and V. Lombardi. 2000. Conformation of the myosin motor during force generation in skeletal muscle. Nat. Struct. Biol. 7:482-485.
9. Piazzesi, G., M. Reconditi, M. Linari, L. Lucii, Y.-B. Sun, T. Narayanan, P. Boesecke, V. Lombardi, and M. Irving. 2002. Mechanism of force generation by myosin heads in skeletal muscle. Nature. 415:659-662.
10. Wakabayashi, K., Y. Ueno, Y. Amemiya, and H. Tanaka. 1988. Intensity changes of actin-based layer lines from frog skeletal muscles during an isometric contraction. In Molecular Mechanism of Muscle Contraction. H. Sugi and G.H. Pollack, editors. Plenum Press, New York, London. 353-367.
11. Yagi, N. 1996. Labelling of thin filaments by myosin heads in contracting and rigor vertebrate skeletal muscles. Acta Cryst. D. 52:1169-1173.
12. Inoue, K., T. Oka, T. Suzuki, N. Yagi, K. Takeshita, S. Goto, and T. Ishikawa. 2001. Present status of high flux beamline (BL40XU) at SPring-8. Nucl. Instr. Method. A467-468:674-677.
13. Yagi, N. 2003. An x-ray diffraction study on early structural changes in skeletal muscle contraction. Biophys. J. 84:1093-1102.
14. Yagi, N., K. Inoue, and T. Oka. 2004. CCD-based x-ray area detectors for time-resolved experiments. J. Synchr. Rad. 11:456-461.
15. Hara, T., T. Tanaka, T. Seike, T. Bizen, X. Maréchal, T. Kohda, K. Inoue, T. Oka, T. Suzuki, N. Yagi, and H. Kitamura. 2001. In-vacuum x-ray helical undulator for high flux beamline at SPring-8. Nucl. Instr. Method. A467-468:165-168.
16. Amemiya, Y., K. Ito, N. Yagi, Y. Asano, K. Wakabayashi, T. Ueki, and T. Endo. 1995. Large-aperture TV detector with a beryllium-windowed image intensifier for x-ray diffraction. Rev. Sci. Instr. 66:2290-2294.
17. Wakayama, J., T. Tamura, N. Yagi, and H. Iwamoto. 2004. Structural transients of contractile proteins upon sudden ATP liberation in skeletal muscle fibers. Biophys. J. 87:430-441.
18. Mendelson, R., and E. P. Morris. 1997. The structure of the actomyosin subfragment 1 complex: results of searches using data from electron microscopy and x-ray crystallography. Proc. Natl. Acad. Sci. USA. 94:8533-8538.
19. Huxley, H. E., and M. Kress. 1985. Crossbridge behavior during muscle contraction. J. Muscle Res. Cell Motil. 6:153-161.
20. Baker, J. E., I. Brust-Mascher, S. Ramachandran, L. E. W. LaConte, and D. D. Thomas. 1998. A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction. Proc. Natl. Acad. Sci. USA. 95:2944-2949.
21. Luther, P. K., and J. M. Squire. 1980. Three-dimensional structure of the vertebrate muscle A-band. II. The myosin filament superlattice. J. Mol. Biol. 141:409-439.
22. Yagi, N., Y. Amemiya, and K. Wakabayashi. 1995. A real-time observation of x-ray diffraction from frog skeletal muscle during and after slow length changes. Jpn. J. Physiol. 45:583-606,
23. Lombardi, V., G. Piazzesi, M. A. Ferenczi, H. Thirlwell, I. Dobbie, and M. Irving. 1995. Elastic distortion of myosin heads and repriming of the working stroke in muscle. Nature. 374:553-555.
24. Huxley, H. E., M. Reconditi, A. Stewart, and T. Irving. 2003. X-ray interference evidence concerning the range of crossbridge movement, and backbone contributions to the meridional pattern. Adv. Exp. Med. Biol. 538:233-241.
25. Haselgrove, J. C. 1975. X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J. Mol. Biol. 92:113-143.
26. Ford, L., A. F. Huxley, and R. M. Simmons. 1977. Tension responses to sudden length change in stimulated frog muscle fibres near slack length. J. Physiol. 269:441-515.
27. Lombardi, V., G. Piazzesi, and M. Linari. 1992. Rapid regeneration of the actin-myosin power stroke in contracting muscle. Nature. 355:638-641.
28. Koubassova, N. A., and A. K. Tsaturyan. 2002. Direct modeling of x-ray diffraction pattern from skeletal muscle in rigor. Biophys. J. 83:1082-1097.
29. Tamura, T., J. Wakayama, T. Fujisawa, N. Yagi, and H. Iwamoto. 2004. Intensity of x-ray reflections from skeletal muscle thin filaments partially occupied with myosin heads: effect of cooperative binding. J. Muscle Res. Cell Motil. 25:329-335.
30. Linari, M., G. Piazzesi, I. Dobbie, N. Koubassova, M. Reconditi, T. Narayanan, O. Diat, M. Irving, and V. Lombardi. 2000. Interference fine structure and sarcomere length dependence of the axial x-ray pattern from active single muscle fibers. Proc. Natl. Acad. Sci. USA. 97:7226-7231.
31. Ferenczi, M. A., S. Y. Bershitsky, N. Koubassova, V. Siththanandan, W. I. Helsby, P. Panine, M. Roessle, T. Narayanan, and A. K. Tsaturyan. 2005. The "roll and lock" mechanism of force generation in muscle. Structure. 13:131-141.
32. Matsubara, I., N. Yagi, and H. Hashizume. 1975. Use of an x-ray television for diffraction of the frog striated muscle. Nature. 255:728-729.
33. Squire, J. M., and J. J. Harford. 1988. Actin filament organization and myosin head labelling patterns in vertebrate skeletal muscles in the rigor and weak binding states. J. Muscle Res. Cell Motil. 9:344-358.