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Phosphorylation of sea urchin sperm H1 and H2B histones precedes chromatin decondensation and H1 exchange during pronuclear formation
Authors:G R Green  D L Poccia
Affiliation:1. Post Graduate Department of Pathology, King George''s Medical University UP, Lucknow, India;2. Department of Physiology, K.G. Medical University UP, Lucknow, India;3. Department of Forensic Medicine & Toxicology, King George''s Medical University UP, Lucknow, India;1. Biosystems Science Course, Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan;2. Department of Biological Sciences, Faculty of Science, Hokkaido University, Sapporo 060-0810, Japan;1. Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA;2. Perlmutter NYU Cancer Center, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA;3. Department of Microbiology, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA;4. Institute for System Genetics, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA;5. Proteomics Resource Center, Office of Collaborative Science, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA;6. Department of Radiation Oncology, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA;7. Howard Hughes Medical Institute, 522 First Avenue, SRB 1107, New York, NY 10016, USA
Abstract:Immediately following fertilization in the sea urchin, sperm-specific histones Sp H1 and Sp H2B are phosphorylated. Then, in parallel with chromatin decondensation, nearly all phosphorylated Sp H1 is lost from the pronuclear chromatin, with the concurrent assimilation of the egg phosphoprotein CS H1. Chemical cleavage of in vivo labeled Sp H1 and Sp H2B shows that serine phosphorylation occurs in the unusually long N-terminal region of these proteins. These regions contain tandemly repeated tetra- and pentapeptide units each containing serine, proline, and two basic amino acids. It is proposed that sperm chromatin decondensation may require prior phosphorylation of these unusual N-terminal regions, whose function in the mature sperm may be to condense or stabilize its highly compact chromatin.
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