The structure of C-protein and X-protein molecules and a polymer of X-protein.

ABSTRACT

C-protein and X-protein are components of the thick filaments in vertebrate skeletal muscles and occupy similar locations in different fibre types. We find that the molecules are both rods about 30 to 40 A wide, but they differ significantly in their lengths, the X-protein molecule being about 350 A long and the C-protein molecule about 280 A. This suggests they are not isoforms. The short length of the C-protein molecule implies that it cannot act in the thick filament as a length-determining agent by a simple vernier mechanism. X-protein associates at low ionic strength (KCl concentration less than 0.07 M) but, unlike C-protein, forms long ordered polymers. These have been examined by electron microscopy to gain information on the molecular shape and on how the molecules interact. The polymers are helically twisted ribbons with a repeat distance along the axis of 660 A. The cross-section of the ribbon is approximately elliptical with major and minor axes of 405 A and 166 A, respectively. From an analysis of the micrographs by optical diffraction, we deduce that the molecules run across the face of the ribbon at an angle of about 15 degrees to the diameter and lie on a two-stranded helix. Models for the polymer are discussed in which the molecules are slightly bowed outwards and bind to each other only at their ends. We suggest that interactions similar to those in the polymer might occur in the thick filaments of muscle, and propose that at each axial position where X-protein attaches along the myosin filament, three X-protein molecules might form an approximately triangular ring around the filament backbone. The appearance of the X-protein polymers is similar to that of the twisted structures called paired helical filaments that make up the neurofibrillary tangles associated with dementia of the Alzheimer type.