Histone H4 acetylation is essential to proceed from a histone- to a protamine-based chromatin structure in spermatid nuclei of Drosophila melanogaster.

@article{Awe2010HistoneHA,
  title={Histone H4 acetylation is essential to proceed from a histone- to a protamine-based chromatin structure in spermatid nuclei of Drosophila melanogaster.},
  author={Stephan Awe and Renate Renkawitz-Pohl},
  journal={Systems biology in reproductive medicine},
  year={2010},
  volume={56 1},
  pages={44-61}
}
In humans, other mammals, and also in Drosophila, the paternal genome in the sperm is highly condensed and organized mainly in a protamine-based chromatin structure. However, the timing and mechanism of the switch from a histone- to the protamine-based chromatin configuration is still poorly understood. We therefore established Drosophila in vitro cultures of cysts with 64 synchronously developing spermatids genetically marked with histone H2AvD-RFP and ProtamineB-eGFP. Live cell imaging showed… CONTINUE READING

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