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Changes in nuclear content of protein conjugate histone H2A—ubiquitin during rooster spermatogenesis
Author(s) -
Agell Neus,
Chiva Manel,
Mezquita Cristóbal
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80604-2
Subject(s) - protamine , spermiogenesis , rooster , histone , spermatogenesis , sperm , ubiquitin , microbiology and biotechnology , biology , nuclear protein , spermatid , biochemistry , chemistry , dna , genetics , gene , endocrinology , heparin , philosophy , theology , transcription factor
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.