Posttranslational modifications of nuclear proteins in rat cerebral hemispheres during postnatal development.
The processes of acetylation, phosphorylation, and methylation of nuclear proteins in cerebral hemispheres of 10- and 30-day-old rats were investigated. The experiments were carried out in vitro by measuring the incorporation of labeled precursors into histones and nonhistone chromosomal proteins (NHP) extracted from nuclei and separated by polyacrylamide gel electrophoresis. The results obtained indicate that there are age-specific differences in the processes of phosphorylation and methylation of chromosomal proteins, whereas the acetylation process did not change significantly between 10 and 30 days of age. Electrophoretic analysis of histones indicated that the histone H3 was labeled to a greater degree than the other fractions and showed major changes in the processes of phosphorylation and methylation during postnatal development. The electrophoretic analysis of NHP showed considerable changes between 10 and 30 days of age. Certain components of NHP became increasingly evident as the brain developed. The methylation of an as yet unidentified protein with a molecular weight of approximately 118,000 daltons occurred at both ages.
D000107:Acetylation; D000367:Age Factors; D000818:Animals; D001921:Brain / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000096:biosynthesis; D004591:Electrophoresis, Polyacrylamide Gel; D008745:Methylation; D009698:Nucleoproteins / Q000096:biosynthesis*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D051381:Rats; D011919:Rats, Inbred Strains
D002868:Chromosomal Proteins, Non-Histone; D009698:Nucleoproteins