Biochemical and structural characterization of actin from Dictyostelium discoideum.

Diaphanous-related formins: characterization of mouse mDia1, and ForA/dDia3 from Dictyostelium discoideum amoebae

(2007) ForA is a Diaphanous-related formin required for directed cell motility in Dictyostelium discoideum. The American Society for Cell Biology, Dijon, France, Dynamic interplay between cytoskeletal and membrane systems, Abstract: 17. (2008) The actinome of Dictyostelium discoideum in comparison to actins and actin-related protein from other organisms. Characterization of the Ste20-like kinas...

Biochemical and structural studies of actomyosin-like proteins from non-muscle cells. II. Purification, properties, and membrane association of actin from amoebae of Dictyostelium discoideum.

Actin, an apparently universal component of eukaryotic cells, has been purified from Dictyostelium amoebae to electrophoretic homogeneity. Purification was facilitated by newly discovered solubility properties of actomyosin in 30% sucrose. A quantitative assay for the Dictyostelium actin is described which is based on its ability to activate muscle heavy meromyosin ATPase activity. The specific...

Characterization of actin variants in Dictyostelium discoideum

Dynacortin is a novel actin bundling protein that localizes to dynamic actin structures.

Dynacortin is a novel protein that was discovered in a genetic suppressor screen of a Dictyostelium discoideum cytokinesis-deficient mutant cell line devoid of the cleavage furrow actin bundling protein, cortexillin I. While dynacortin is highly enriched in the cortex, particularly in cell-surface protrusions, it is excluded from the cleavage furrow cortex during cytokinesis. Here, we describe ...

Isolation and Characterization of a 30,000-dalton Calcium-sensitive Actin Cross-linking Protein from Dictyostelium discoideurn”

A calcium-sensitive actin-binding protein having a subunit molecular mass of 3 0 , 0 0 0 daltons (30K protein) has been isolated from Dictyostelium discoideum. Structural, immunological, and functional analyses demonstrated that the 30K protein was distinct from other actin-binding proteins of D. discoideum. A native molecular mass of 31,700 daltons was determined by equilibrium sedimentation, ...