Different Myosin Head Conformations in Bony Fish Muscles Put into Rigor at Different Sarcomere Lengths

International Journal of Molecular Sciences
Felicity EakinsJohn M Squire

Abstract

At a resting sarcomere length of approximately 2.2 µm bony fish muscles put into rigor in the presence of BDM (2,3-butanedione monoxime) to reduce rigor tension generation show the normal arrangement of myosin head interactions with actin filaments as monitored by low-angle X-ray diffraction. However, if the muscles are put into rigor using the same protocol but stretched to 2.5 µm sarcomere length, a markedly different structure is observed. The X-ray diffraction pattern is not just a weaker version of the pattern at full overlap, as might be expected, but it is quite different. It is compatible with the actin-attached myosin heads being in a different conformation on actin, with the average centre of cross-bridge mass at a higher radius than in normal rigor and the myosin lever arms conforming less to the actin filament geometry, probably pointing back to their origins on their parent myosin filaments. The possible nature of this new rigor cross-bridge conformation is discussed in terms of other well-known states such as the weak binding state and the 'roll and lock' mechanism; we speculate that we may have trapped most myosin heads in an early attached strong actin-binding state in the cross-bridge cycle on actin.

References

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Citations

Jul 22, 2019·Journal of Muscle Research and Cell Motility·Felicity EakinsJohn M Squire
Nov 20, 2019·International Journal of Molecular Sciences·John Squire
Aug 6, 2021·The Journal of General Physiology·John M Squire, Carlo Knupp

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Methods Mentioned

BETA
electron microscopy
protein
X-ray
dissection

Software Mentioned

FibreFix
Peakfit
Synthseries
FSYNTH

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