Analysis of cytoplasmic 19 S ring-type particles in Drosophila which contain hsp 23 at normal growth temperature Export

@article{citeulike:1274508, abstract = {Cytoplasmic 19 S particles were isolated from postpolysomal supernatants of 25[degree sign]C Drosophila embryos and culture cells. The particles were purified by salt extraction and sucrose gradient centrifugation. Electron microscopic investigation showed that the 19 S particles possess a ring-shaped morphology with an outer diameter of 12 nm and a hollow core of 3 nm. Biochemically the particles are characterized by a group of 16 polypeptides within the molecular weight range of 35 to 23 kDa, and small RNA molecules in the size range of 200 to 60 nucleotides. The RNP character of the particles is also shown by their buoyant density in Cs2SO4 of [varrho] = 1.29 g/cm3 and their susceptibility to uv crosslinking and density in CsCl of [varrho] = 1.38 g/cm3. Antibodies were raised against the proteins of the 19 S particles isolated from 25[degree sign]C cells and tested by immunoblotting after one- and two-dimensional gelelectrophoresis. Two of the antibodies raised cross react with the small heat-shock proteins hsp 28/27 and hsp 23. Comparative protease V8 cleavage of hsp 23 and the 23-kDa particle protein demonstrates that these two proteins are identical and that the small hsp of Drosophila must be a genuine part of the 19 S cytoplasmic ring-shaped complexes at normal growth temperature. The data support the idea of a general developmental role of some of the so-called heat-shock proteins.}, author = {Schuldt, Claus and Kloetzel, Peter-M}, citeulike-article-id = {1274508}, citeulike-linkout-0 = {http://www.sciencedirect.com/science/article/B6WDG-4DV05FN-FJ/2/383d1d5ddaab68e5dbdbf65e466d0f81}, journal = {Developmental Biology}, keywords = {drosophila, proteasome}, month = {July}, number = {1}, pages = {65--74}, posted-at = {2007-05-03 19:22:14}, priority = {2}, title = {Analysis of cytoplasmic 19 S ring-type particles in Drosophila which contain hsp 23 at normal growth temperature}, url = {http://www.sciencedirect.com/science/article/B6WDG-4DV05FN-FJ/2/383d1d5ddaab68e5dbdbf65e466d0f81}, volume = {110}, year = {1985} }

TY - JOUR ID - citeulike:1274508 L3 - citeulike-article-id:1274508 N2 - Cytoplasmic 19 S particles were isolated from postpolysomal supernatants of 25[degree sign]C Drosophila embryos and culture cells. The particles were purified by salt extraction and sucrose gradient centrifugation. Electron microscopic investigation showed that the 19 S particles possess a ring-shaped morphology with an outer diameter of 12 nm and a hollow core of 3 nm. Biochemically the particles are characterized by a group of 16 polypeptides within the molecular weight range of 35 to 23 kDa, and small RNA molecules in the size range of 200 to 60 nucleotides. The RNP character of the particles is also shown by their buoyant density in Cs2SO4 of [varrho] = 1.29 g/cm3 and their susceptibility to uv crosslinking and density in CsCl of [varrho] = 1.38 g/cm3. Antibodies were raised against the proteins of the 19 S particles isolated from 25[degree sign]C cells and tested by immunoblotting after one- and two-dimensional gelelectrophoresis. Two of the antibodies raised cross react with the small heat-shock proteins hsp 28/27 and hsp 23. Comparative protease V8 cleavage of hsp 23 and the 23-kDa particle protein demonstrates that these two proteins are identical and that the small hsp of Drosophila must be a genuine part of the 19 S cytoplasmic ring-shaped complexes at normal growth temperature. The data support the idea of a general developmental role of some of the so-called heat-shock proteins. IS - 1 JF - Developmental Biology EP - 74 TI - Analysis of cytoplasmic 19 S ring-type particles in Drosophila which contain hsp 23 at normal growth temperature VL - 110 SP - 65 KW - drosophila KW - proteasome AU - Schuldt, Claus AU - Kloetzel, Peter-M PY - 1985/07// UR - http://www.sciencedirect.com/science/article/B6WDG-4DV05FN-FJ/2/383d1d5ddaab68e5dbdbf65e466d0f81 ER -