Isolation of four core histones from human sperm chromatin representing a minor subset of somatic histones

• Published in: The Journal of biological chemistry Vol. 265; no. 33; pp. 20662 - 20666
• Main Authors: Gatewood, J M, Cook, G R, Balhorn, R, Schmid, C W, Bradbury, E M
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.11.1990; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acids - analysis; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Chromatin - chemistry; Chromatography, High Pressure Liquid; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Genetic Variation; Histones - isolation & purification; Holoproteins; Humans; Male; Molecular Weight; Nuclear proteins; Proteins; Spermatozoa - chemistry; Human; Chromatin; Spermatozoa; Purification; Histone H2A; Gel electrophoresis; Immunocytochemistry; HPLC chromatography; Two dimensional electrophoresis
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(17)30554-9

Using high performance liquid chromatography we have successfully purified four core histones from mature human sperm chromatin. The H2A variants present in sperm (H2A.X and limited H2A.Z) have been shown previously to be minor variants in somatic chromatin. The histones are highly modified as evidenced by extensive acetylation and an as yet uncharacterized multicharge modification of H2B. Based on our data, we conclude that histone proteins are a minor component of each mature spermatozoa. Given the unique nature of the histone variants present in sperm, we propose that this chromatin component has a specific function and may possibly facilitate the programming of genes which will be active in early development.