Phosphorylation of sea urchin sperm H1 and H2B histones precedes chromatin decondensation and H1 exchange during pronuclear formation.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D003488:Cyanogen Bromide; D005260:Female; D005306:Fertilization; D006657:Histones / Q000378:metabolism*; D008297:Male; D010446:Peptide Fragments / Q000032:analysis; D010750:Phosphoproteins / Q000032:analysis; D010766:Phosphorylation; D012617:Sea Urchins; D013094:Spermatozoa / Q000378:metabolism*
D002843:Chromatin; D006657:Histones; D010446:Peptide Fragments; D010750:Phosphoproteins; D003488:Cyanogen Bromide