Changes in nuclear content of protein conjugate histone H2A-ubiquitin during rooster spermatogenesis.
Electrophoretic analysis of acid-soluble chromosomal proteins isolated from rooster testis cell nuclei at different stages of spermatogenesis, revealed that the nuclear content of a protein identified by its solubility, electrophoretic mobility and amino acid analysis as the protein conjugate histone H2A-ubiquitin (uH2A, A24) changed markedly from meiotic cells to late spermatids. The protein was not detectable in tetraploid primary spermatocytes; it was present in 1.7% of the total amount of nucleosomal core histones in early spermatids and reached its maximum level (3.5% and 11%) at the end of spermiogenesis, when histones are replaced by the protamine galline.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D002645:Chickens; D002868:Chromosomal Proteins, Non-Histone / Q000302:isolation & purification / Q000378:metabolism*; D004586:Electrophoresis; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism*; D008297:Male; D013091:Spermatogenesis; D013737:Testis / Q000378:metabolism*; D014452:Ubiquitins
D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D014452:Ubiquitins; C021645:chromatin conjugate protein A24