Overproduction of an 85-kD yeast actin-binding protein caused a reorganization of the actin cytoskeleton, dramatically affecting the budding pattern and spatial growth organization of the yeast cell.
Identification and overproduction of an 85-kD yeast actin-binding protein demonstrates its role as a determinant of growth sites and morphogenesis.
Three yeast actin-binding proteins were identified using yeast actin filaments as an affinity matrix. One protein appears to be a yeast myosin heavy chain; it is dissociated from actin filaments by ATP, it is similar in size (200 kD) to other myosins, and antibodies directed against Dictyostelium myosin heavy chain bind to it. Immunofluorescence experiments show that a second actin-binding protein (67 kD) colocalizes in vivo with both cytoplasmic actin cables and cortical actin patches, the only identifiable actin structures in yeast. The cortical actin patches are concentrated at growing surfaces of the yeast cell where they might play a role in membrane and cell wall insertion, and the third actin-binding protein (85 kD) is only detected in association with these structures. This 85-kD protein is therefore a candidate for a determinant of growth sites. The in vivo role of this protein was tested by overproduction; this overproduction causes a reorganization of the actin cytoskeleton which in turn dramatically affects the budding pattern and spatial growth organization of the yeast cell.
Drubin et al. (Thu,) reported a other. Overproduction of 85-kD actin-binding protein was evaluated on Reorganization of the actin cytoskeleton, budding pattern, and spatial growth organization. Overproduction of an 85-kD yeast actin-binding protein caused a reorganization of the actin cytoskeleton, dramatically affecting the budding pattern and spatial growth organization of the yeast cell.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: