Abstract
Decondensation of sperm chromatin in cell-free Drosophila embryo extracts was efficient, rapid, and synchronous. The decondensation activity was N-ethylmaleimide-resistant, soluble, and heat-stable. Two specific proteins, X and Y, were removed selectively from Xenopus sperm coincident with morphological decondensation. A heat-stable protein, p22, was purified to apparent homogeneity from Drosophila melanogaster embryos by a procedure optimized for the purification of Xenopus laevis nucleoplasmin. Although itself capable of catalyzing decondensation of Xenopus sperm, the precise relationship of Drosophila p22 to Xenopus nucleoplasmin is unclear. Drosophila p22 and Xenopus nucleoplasmin were immunologically distinct. Moreover, p22 was present as a nuclear protein throughout Drosophila development as determined both by immunoblot and by indirect immunofluorescence analyses. Drosophila embryo extracts largely or completely immunodepleted of p22 lost some but not all heat-stable decondensation activity. These observations lead to the conclusion that Drosophila embryo extracts contain at least two heat-stable sperm decondensation factors.
