Driving filament sliding: Weak binding cross-bridge states, strong binding cross-bridge states, and the power stroke

Advances in Experimental Medicine and Biology

Volumn 565, Issue , 2005, Pages 75-91

  Brenner, Bernhard ^a   Mählmann, Enke ^a   Mattei, Thomas ^a   Kraft, Theresia ^a  

^a HANNOVER MEDICAL SCHOOL   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); ADENOSINE TRIPHOSPHATE; CALCIUM ION; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; TROPOMYOSIN; CALCIUM;

ACTIN FILAMENT; ACTIN MYOSIN INTERACTION; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; FLUORESCENCE; IONIC STRENGTH; MUSCLE CONTRACTION; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN BINDING; PSOAS MUSCLE; RABBIT; TEMPERATURE SENSITIVITY; THIN FILAMENT; X RAY DIFFRACTION; ANIMAL; ARTICLE; BIOLOGICAL MODEL; CHEMISTRY; DRUG EFFECT; KINETICS; MECHANICAL STRESS; METABOLISM; MUSCLE CELL; PHYSIOLOGY; PROTEIN CONFORMATION; SKELETAL MUSCLE;

ACTINS; ANIMALS; CALCIUM; KINETICS; MODELS, BIOLOGICAL; MUSCLE CONTRACTION; MUSCLE FIBERS; MUSCLE, SKELETAL; MYOSINS; PROTEIN BINDING; PROTEIN CONFORMATION; RABBITS; STRESS, MECHANICAL; X-RAY DIFFRACTION;

EID: 33644792492     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/0-387-24990-7_7     Document Type: Conference Paper

References (38)

1. ++-dependent ATPase of myosin and its proteolytic fragments. Cold Spring Harb Symp Quant Biol 37: 127-135, 1973.
2. Brenner B, Schoenberg M, Chilovich JM, Greene LC, and Eisenberg E. Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. Proc Natl Acad Sci USA 79:7288-7291, 1982.
3. Brenner B, Yu LC, and Podolsky RJ. X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths. Biophys J 46:299-306, 1984.
4. Brenner B, and Yu LC. Equatorial X-ray diffraction from single skinned rabbit psoas fiber at various degrees of activation. Changes in intensities and lattice spacing. Biophys J 48:829-834, 1985.
5. i solutions. Biophys J 50:685-691, 1986.
6. i in skinned rabbit psoas fibers. Biophys J 50:1101-1108, 1986(b).
7. Brenner B. Muscle mechanics and biochemical kinetics, in: Molecular Mechanism of Muscular Contraction, John Squire, ed., Macmillan Press Ltd., London, pp. 77-149, 1990.
8. Brenner B, Yu LC, and Chalovich JM. Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon. Implications for the pathway to force generation. Proc Natl Acad Sci USA 88:5739-5743, 1991.
9. Brenner B, Chalovich JM, and Yu LC. Distinct molecular processes associated with isometric force generation and with rapid tension recovery after quick release. Biophys J 68:106s-111s, 1995.
10. Brenner B, Kraft T, and Chalovich JM. Fluorescence of NBD-labeled troponin-I as a probe for the kinetics of thin filament activation. Adv Exp Med Mol Biol 453:177-185, 1998.
11. Brenner B, and Chalovich JM. Kinetics of thin filament activation probed by fluorescence of N-((2-Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1, 3-diazole-labelled troponin I incorporated in skinned fibers of rabbit psoas muscle. Implications for regulation of muscle contraction. Biophys J 77:2692-2708, 1999.
12. Brenner B, Kraft T, Yu LC and Chalovich JM. Thin filament activation probed by fluorescence of N-((2-Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2- oxa-1,3-diazole-labelled troponin I incorporated in skinned fibers of rabbit psoas muscle. Biophys J 77:2677-2691, 1999.
13. Chase PB, Martyn DA, Kushmerick MJ, and Gordon AM. Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibres from rabbit. J Physiol Lond 460:231-46, 1993.
14. Dantzig JA, Goldman YE, Millar NC, Lacktis J, and Homsher E. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J Physiol Lond 451:247-278, 1992.
15. ++ in skinned fibers of rabbit psoas muscle. Biophys 72:2255-2261, 1997.
16. Geeves MA, Goody RS, and Gutfreund H. Kinetics of acto.S1 interaction. J Muscle Res Cell Motil 5:351-361, 1984.
17. Geeves MA, and Conibear PB. The role of three state docking of myosin S1 with actin in force generation. Biophys J 68:194s-201s, 1995.
18. Goody RS, and Hofmann F. Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides J Muscle Res Cell Motil 1:101-115, 1980.
19. Greene LE, and Eisenberg E. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc Natl Acad Sci USA: 77:2616-2620, 1980.
20. Greene LE, Sellers JR, Eisenberg E, and Adelstein RS. Binding of gizzard smooth muscle myosin subfragment-one to actin in the presence and absence of ATP. Biochemistry 22:530-535, 1983.
21. Gu J, Xu S, and Yu LC. A model of cross-bridge attachment to actin in the A‡M‡ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle. Biophys J 82:2123-33, 2002.
22. Head JG, Ritchie MD, and Geeves MA. Characterization of the equilibrium between blocked and closed states of muscle thin filaments. Eur J Biochem 227:694-699, 1995.
23. Holmes KC. The actomyosin interaction and its control by tropomyosin. Biophys J 68:2s-5s, 1995.
24. ++ on weak cross-bridge interaction with actin in the presence of the nucleotide analog ATPγS. Proc Natl Acad Sci USA 89:11362-11366, 1992.
25. Kraft T, Chalovich JM, Yu LC, and Brenner B. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological temperature and ionic strength conditions. Additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. Biophys J 68:2404-2418, 1995.
26. Kraft T, Xu S, Brenner B, and Yu LC. The effect of thin filament activation on the attachment of weak binding cross-bridges: A 2D-Xray-diffraction study on single muscle fibers. Biophys J 76:1494-1513, 1999.
27. Kraft T, Mattel T, Radocaj A, Piep B, Nocula Ch, Furch M, and Brenner B. Structural features of cross-bridges in isometrically contracting skeletal muscle. Biophys J 82:2536-2547, 2002.
28. Kraft T, Mählmann E, Mattel T, and Brenner B. Effects of myosin binding to actin on structural and functional properties of the myosin head domain. Biophys J 86:266a, 2004.
29. 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 368:65-67, 1994.
30. Lehman W, Vibert P, Uman P, and Craig R. Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J Mol Biol 251:191-196, 1995.
31. 4-binding to cross-bridges under rigor conditions: mechanical and structural properties of the resulting cross-bridge state. Biophys J 86:266a, 2004.
32. McKillop DFA, and Geeves MA. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J 65:693-701, 1993.
33. Millar NC, and Homsher E. The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. A steady state and transient kinetic study. J Biol Chem 265:20234-20240, 1990.
34. Schoenberg M. Equilibrium muscle cross-bridge behavior. Theoretical considerations. Biophys J 48:467-475, 1985.
35. Stein LA, Schwartz RP, Chock PB, and Eisenberg E. Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5′-triphosphate hydrolysis can occur without dissociation of the actomyosin complex. Biochemistry 18:3895-3909, 1979.
36. Stein LE, Chock PB, and Eisenberg E. The rate-limiting step in the actomyosin adenosintriphosphatase cycle. Biochemistry 23:1555-1563, 1984.
37. White HD, and Taylor EW. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry 15:5818-5826, 1976.
38. Xu S, Malinchik S, Gilroy D, Kraft T, Brenner B, and Yu LC. X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle. Biophys J 72:2292-2303, 1997.