Effect of post-synthetic modifications of proteins on the binding of estrogen-receptor complex to uterine nuclei of aging rats.
The binding of estrogen-receptor (ER) complex to nuclei following post-synthetic modifications of proteins was examined in the uteri of young (18 weeks) and old (96 weeks) rats. Acetylation decreases the binding of ER complex to nuclei but methylation shows no effect on the extent of binding in both ages. On the other hand, phosphorylation enhances the binding of ER complex by two-fold in nuclei from young rats but reduces this to half in nuclei from old rats. The pattern of binding in salt-resistant nuclear fractions is similar to that in total nuclei except in methylation where old rats show about 20% higher binding as compared to the respective control. These findings suggest that post-synthetic modifications of proteins modulate the binding of ER complex to uterine nuclei in an age-specific manner.
Kaur
J
J
Department of Zoology, Banaras Hindu University, Varanasi, India.
Thakur
M K
MK
D000107:Acetylation; D000375:Aging / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D002467:Cell Nucleus / Q000378:metabolism*; D004958:Estradiol / Q000378:metabolism; D005260:Female; D066298:In Vitro Techniques; D008745:Methylation; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D051381:Rats; D011919:Rats, Inbred Strains; D011960:Receptors, Estrogen / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D014599:Uterus / Q000378:metabolism*
D011960:Receptors, Estrogen; D004958:Estradiol