Nuclear protein changes in the maternally and paternally derived chromatin at fertilization.
The proteins which become associated with the paternally derived chromatin during fertilization may be instrumental in its activation and in the dramatic structural metamorphosis of the sperm nucleus during pronuclear development. Proteins associated with sperm and zygote nuclei and male and female pronuclei of fertilized sea urchin eggs were analysed by polyacrylamide gel electrophoresis in order to examine nuclear protein changes in the paternally and maternally derived chromatin following insemination. Results demonstrate major changes in both the solubility characteristics and polypeptide profiles of sperm nuclei upon insemination. Evidence is presented which indicates that at fertilization the paternally derived chromatin acquires proteins of molecular weights greater than 80,000 and a nuclear protein composition similar to that of the female pronucleus. The nuclear proteins associated with zygote nuclei were compared to those of combined male and female pronuclei and showed many similarities and some differences. Several polypeptides were present in zygote nuclei which were not observed in pronuclear extracts.
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D002843:Chromatin / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005306:Fertilization; D008297:Male; D009698:Nucleoproteins / Q000032:analysis; D012617:Sea Urchins; D013094:Spermatozoa / Q000032:analysis; D015053:Zygote / Q000032:analysis
D002843:Chromatin; D009698:Nucleoproteins