An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments.

Abstract

The interaction of fructose diphosphate aldolase [beef skeletal muscle] with F-actin, F-actin-tropomyosin and F-actin-tropomyosin-troponin was studied by using negative staining. In the absence of troponin, minor aggregates of aldolase and the F-actin filaments were formed. A well-ordered lattice structure was only formed in the case of the fully reconstituted filament when the filament-to-filament spacing is 18 nm and the cross-bridge spacing was 38.7 nm. The lattice was due to an interaction between troponin and aldolase. The minimum subunit structure of troponin, still capable of giving rise to a lattice, was the troponin-IT complex, which indicated that troponin-C was not involved in aldolase binding.