Stimulation of the interaction between actin and myosin by Physarum caldesmon-like protein and smooth muscle caldesmon.
作者： R. Ishikawa , T. Okagaki , S. Higashi-Fujime , K. Kohama
DOI: 10.1016/S0021-9258(18)54705-0
关键词: Actin 、 Caldesmon 、 Biology 、 Motility 、 Tropomyosin 、 Binding protein 、 Physarum polycephalum 、 Myosin 、 Physarum 、 Biophysics 、 Biochemistry
摘要: We have purified an actin-binding protein from the plasmodia of a lower eukaryote, Physarum polycephalum, with apparent molecular mass 210,000 daltons on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This bound to actin filaments stoichiometry 1:7-8 in Ca(2+)-calmodulin-dependent manner. Antibody raised against caldesmon smooth muscle cross-reacted 210-kDa protein. In vitro motility assay revealed that increased sliding velocity myosin. The more than doubled actin-activated ATPase activity myosin under comparative conditions assay. Further increases concentration decreased its stimulatory effects. Ca(2+)-calmodulin prevented effects Unexpectedly, also at concentrations. well-known inhibitory effect actin-myosin interaction was observed this when further. and were confirmed by measurements From estimations intracellular concentrations vivo, it appears former latter interactions vivo are inhibitory, respectively.
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