Key result
A 30,000-dalton protein isolated from Dictyostelium crosslinks actin filaments, affects low shear viscosity, and is insensitive to calcium.
Answers are grounded in this paper and cite their sources.
The study identifies a novel 30,000-dalton calcium-insensitive actin-crosslinking protein in Dictyostelium discoideum, distinct from previously known actin-binding proteins.
We have isolated a 30,000-dalton protein from Dictyostelium which cosedimented with and affected the low shear viscosity of actin. At low concentrations, this protein increased the low shear viscosity to greater than that of the actin control, whereas higher concentrations decreased viscosity. The viscosity decrease correlated with the formation of actin filament bundles, as seen electron microscopically. This protein resembled a previously reported actin-binding protein from Dictyostelium [Fechheimer and Taylor, 84, J Biol Chem 259:4514] in electrophoretic mobility, Stokes radius, and ability to crosslink filaments, but was shown to be different by peptide mapping, lack of immunologic crossreactivity, and lack of sensitivity to calcium.
No takes yet. Share an insight, caveat, or question.
Susan S. Brown (1985) studied this question. 30,000-dalton protein from Dictyostelium vs. actin control was evaluated on low shear viscosity of actin and formation of actin filament bundles. A 30,000-dalton protein isolated from Dictyostelium crosslinks actin filaments, affects low shear viscosity, and is insensitive to calcium.
Synapse has enriched 10 related papers. Consider them for comparative context: