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PMID: 1742454 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Biophysical journal ·Vol. 60 ·No. 4 ·1991-10-00 ·Pages 812-24

Lowy J, Popp D, Stewart AA

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.

MeSH Terms
Actins/metabolism Adenosine Triphosphate/metabolism Animals In Vitro Techniques Muscle Relaxation Muscles/physiology Myosin Subfragments/metabolism Myosins/chemistry,metabolism Rabbits Thermodynamics X-Ray Diffraction/methods
Chemicals
Actins Myosin Subfragments Adenosine Triphosphate Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lowy J
Open University Research Unit, Oxford, United Kingdom.
Popp D
Stewart A A
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1991-10-00
Pages
812-24
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1260133
Subset
IM
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