Changes in nuclear content of protein conjugate histone H2A-ubiquitin during rooster spermatogenesis.

Abstract

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.

• Authors: N Agell, M Chiva, C Mezquita
• Journal: FEBS letters (FEBS Lett) Vol. 155 Issue 2 Pg. 209-12 (May 08 1983) ISSN: 0014-5793 [Print] England
• PMID: 6303842 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Chromosomal Proteins, Non-Histone
• Histones
• Ubiquitins
• chromatin conjugate protein A24

Topics

• Animals
• Cell Nucleus (metabolism)
• Chickens
• Chromosomal Proteins, Non-Histone (isolation & purification, metabolism)
• Electrophoresis
• Histones (isolation & purification, metabolism)
• Male
• Spermatogenesis
• Testis (metabolism)
• Ubiquitins