Comparative studies of rat liver and sea urchin embryo nuclear matrices: partial fractionation and protein kinase activity distribution.
Rat liver and sea urchin embryo nuclear matrices were found to differ in composition and in the strength of the association of their structural elements. Apart from the qualitative differences in composition, the embryonic matrices retained greater amounts of nuclear proteins and DNA, and were less susceptible to ultrasonic treatment than those of rat liver. They were essentially resistant to mild sonication, by which the rat liver matrix structure was resolved into two distinct fractions, referred to by Berezney (1980) as matricin and ribonucleoprotein (RNP). Both sub-fractions exhibited a protein kinase activity; the phosphorylating capacity of the RNP-associated protein kinases was found to be higher than that of the matricin-bound enzyme. The preferred substrate was among the secondary matrix proteins. In sea urchin embryos, sonication introduced no change in the type and lesion of the matrix proteins phosphorylated by the associated enzyme.
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D004247:DNA / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000032:analysis* / Q000196:embryology; D010455:Peptides / Q000032:analysis; D010766:Phosphorylation; D011494:Protein Kinases / Q000032:analysis; D011506:Proteins / Q000032:analysis; D012313:RNA / Q000032:analysis; D051381:Rats; D012261:Ribonucleoproteins / Q000032:analysis; D012617:Sea Urchins / Q000032:analysis* / Q000196:embryology
D010455:Peptides; D011506:Proteins; D012261:Ribonucleoproteins; D012313:RNA; D004247:DNA; D011494:Protein Kinases