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. 1995 Apr 18;14(8):1711–1717. doi: 10.1002/j.1460-2075.1995.tb07160.x

DF 31, a sperm decondensation factor from Drosophila melanogaster: purification and characterization.

G Crevel 1, S Cotterill 1
PMCID: PMC398264  PMID: 7737122

Abstract

We have purified to homogeneity a Drosophila protein which is able to decondense Xenopus sperm chromatin. This protein, which we have called DF 31, is a heat-stable phosphoprotein which displays a molecular weight of 31 kDa on SDS-PAGE, but which has an apparent molecular weight of > 200 kDa on gel filtration. We show that DF 31 decondenses sperm DNA by displacement of sperm-specific proteins. In addition to its sperm decondensation activity, DF 31 is also able to facilitate nucleosome loading on both decondensed sperm DNA and on naked DNA template. The reaction as catalysed by DF 31 is quite efficient; however, the nucleosomes appear to be loaded randomly onto the DNA, not in regular arrays. Although the mechanism by which DF 31 aids nucleosome loading is not yet clear, it most probably occurs through binding of DF 31 to core histones.

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