Characterization of DNA-protein complexes from the mitochondria of Xenopus laevis oocytes.
Mitochondrial DNA (mtDNA)-protein complexes (nucleoids) from Xenopus laevis oocytes were purified either on rate-zonal sucrose or isopyknic metrizamide gradients. From electron microscopic studies and staphylococcal nuclease digestion experiments mtDNA appears to be packaged into regular beaded structures. Protein electrophoretic analysis and M banding results show that mtDNA is associated with the membrane structures and also with few specific proteins including one acid-soluble polypeptide of 28 kD.
D000818:Animals; D002458:Cell Fractionation / Q000379:methods; D002500:Centrifugation, Isopycnic; D002501:Centrifugation, Zonal; D004272:DNA, Mitochondrial / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007425:Intracellular Membranes / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis; D008836:Micrococcal Nuclease; D008854:Microscopy, Electron; D008928:Mitochondria / Q000032:analysis / Q000648:ultrastructure*; D009865:Oocytes / Q000032:analysis* / Q000648:ultrastructure; D011485:Protein Binding; D011506:Proteins / Q000032:analysis*; D012995:Solubility; D014982:Xenopus laevis
D004272:DNA, Mitochondrial; D008565:Membrane Proteins; D011506:Proteins; D008836:Micrococcal Nuclease