Literature DB >> 1742454

X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles.

J Lowy1, D Popp, A A Stewart.   

Abstract

Using x-rays from a laboratory source and an area detector, myosin layer lines and the diffuse scattering between them in the moderate angle region have been recorded. At full overlap, incubation of rigor muscles with S-1 greatly reduces the diffuse scattering. Also, three of the four actin-based layer lines lying close to the meridian (Huxley, H. E., and W. Brown, 1967. J. Mol. Biol. 30:384-434; Haselgrove, J. C. 1975. J. Mol. Biol. 92:113-143) increase, suggesting fuller labeling of the actin filaments. These results are consistent with the idea (Poulsen, F. R., and J. Lowy, 1983. Nature [Lond.]. 303:146-152) that some of the diffuse scattering in rigor muscles is due to a random mixture of actin monomers with and without attached myosin heads (substitution disorder). In relaxed muscles, regardless of overlap, lowering the temperature from 24 to 4 degrees C practically abolishes the myosin layer lines (a result first obtained by Wray, J.S. 1987. J. Muscle Res. Cell Motil. 8:62 (a). Abstr.), whilst the diffuse scattering between these layer lines increases appreciably. Similar changes occur in the passage from rest to peak tetanic tension in live frog muscle (Lowy, J., and F.R. Poulsen. 1990. Biophys. J. 57:977-985). Cooling the psoas demonstrates that the intensity relation between the layer lines and the diffuse scattering is of an inverse nature, and that the transition occurs over a narrow temperature range (12-14 degrees C) with a sigmoidal function. From these results it would appear that the helical arrangement of the myosin heads is very temperature sensitive, and that the disordering effect does not depend on the presence of actin. Measurements along the meridian reveal that the intensity of the diffuse scattering increases relatively little and does so in a nearly linear manner: evidently the axial order of the myosin heads is much less temperature sensitive. The combined data support the view (Poulsen, F. R., and J. Lowy. 1983. Nature [Lond.]. 303:146-152) that in relaxed muscles a significant part of the diffuse scattering originates from disordered myosin heads. The observation that the extent of the diffuse scattering is greater in the equatorial than in the meridional direction suggests that the disordered myosin heads have an orientation which is on average more parallel to the filament axis.

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Year:  1991        PMID: 1742454      PMCID: PMC1260133          DOI: 10.1016/S0006-3495(91)82116-6

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  29 in total

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Authors:  G F ELLIOTT
Journal:  Proc R Soc Lond B Biol Sci       Date:  1964-10-27

Review 2.  Crossbridge behaviour during muscle contraction.

Authors:  H E Huxley; M Kress
Journal:  J Muscle Res Cell Motil       Date:  1985-04       Impact factor: 2.698

Review 3.  Actin filament organization and myosin head labelling patterns in vertebrate skeletal muscles in the rigor and weak binding states.

Authors:  J M Squire; J J Harford
Journal:  J Muscle Res Cell Motil       Date:  1988-08       Impact factor: 2.698

4.  Domain structure of the myosin head in correlation-averaged images of shadowed molecules.

Authors:  P J Vibert
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5.  Structures of actomyosin crossbridges in relaxed and rigor muscle fibers.

Authors:  L C Yu; B Brenner
Journal:  Biophys J       Date:  1989-03       Impact factor: 4.033

6.  The time course of changes in the equatorial diffraction patterns from different muscle types on photolysis of caged-ATP.

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Journal:  Adv Exp Med Biol       Date:  1988       Impact factor: 2.622

7.  Temperature-induced change of thick filament and location of the functional sites of myosin.

Authors:  T Wakabayashi; T Akiba; K Hirose; A Tomioka; M Tokunaga; M Suzuki; C Toyoshima; K Sutoh; K Yamamoto; T Matsumoto
Journal:  Adv Exp Med Biol       Date:  1988       Impact factor: 2.622

8.  The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor.

Authors:  H E Huxley; W Brown
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9.  Disorder induced in nonoverlap myosin cross-bridges by loss of adenosine triphosphate.

Authors:  R Padrón; R Craig
Journal:  Biophys J       Date:  1989-11       Impact factor: 4.033

10.  Muscle contraction and free energy transduction in biological systems.

Authors:  E Eisenberg; T L Hill
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  24 in total

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2.  A model of cross-bridge attachment to actin in the A*M*ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle.

Authors:  Jin Gu; Sengen Xu; Leepo C Yu
Journal:  Biophys J       Date:  2002-04       Impact factor: 4.033

3.  Changes in myosin S1 orientation and force induced by a temperature increase.

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4.  Orientation of the N-terminal lobe of the myosin regulatory light chain in skeletal muscle fibers.

Authors:  Daniela Romano; Birgit D Brandmeier; Yin-Biao Sun; David R Trentham; Malcolm Irving
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5.  Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.

Authors:  Sergey Y Bershitsky; Natalia A Koubassova; Pauline M Bennett; Michael A Ferenczi; Dmitry A Shestakov; Andrey K Tsaturyan
Journal:  Biophys J       Date:  2010-09-22       Impact factor: 4.033

6.  Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethylrhodamine.

Authors:  C Sabido-David; B Brandmeier; J S Craik; J E Corrie; D R Trentham; M Irving
Journal:  Biophys J       Date:  1998-06       Impact factor: 4.033

7.  X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle.

Authors:  S Xu; S Malinchik; D Gilroy; T Kraft; B Brenner; L C Yu
Journal:  Biophys J       Date:  1997-11       Impact factor: 4.033

8.  Structure and periodicities of cross-bridges in relaxation, in rigor, and during contractions initiated by photolysis of caged Ca2+.

Authors:  T D Lenart; J M Murray; C Franzini-Armstrong; Y E Goldman
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

9.  The effects of changes in temperature or ionic strength on isolated rabbit and fish skeletal muscle thick filaments.

Authors:  R W Kensler; S Peterson; M Norberg
Journal:  J Muscle Res Cell Motil       Date:  1994-02       Impact factor: 2.698

10.  Myosin ATP turnover rate is a mechanism involved in thermogenesis in resting skeletal muscle fibers.

Authors:  Melanie A Stewart; Kathleen Franks-Skiba; Susan Chen; Roger Cooke
Journal:  Proc Natl Acad Sci U S A       Date:  2009-12-04       Impact factor: 11.205

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