Abstract
During spermiogenesis in most vertebrates, the structure of spermatid chromatin is completely reorganized and the DNA is repackaged by a small, arginine-rich protein called protamine. As a consequence of the interactions that occur between DNA and protamine in late-step spermatids [1], the phosphodiester backbone of DNA is neutralized and the fibers of double-helical DNA and protamine coalesce into a maximally condensed [2], biochemically inert state. The resulting DNA-protamine complex is insoluble, enzymatic processes such as DNA repair are inhibited [3,4], and the genome is rendered genetically inactive [5]. Although we have learned a great deal about the structure, metabolism, and potential function of the protamines in the past two decades, we have learned comparatively little about the actual molecular structure of the DNA-protamine complex. The marked insolubility of sperm chromatin and the high affinity of protamine for DNA have often made it difficult to characterize the structure of sperm chromatin using the biochemical and physical techniques that have been applied to somatic chromatin and other DNA-protein complexes.
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Balhorn, R. (1989). Mammalian Protamines: Structure and Molecular Interactions. In: Adolph, K.W. (eds) Molecular Biology of Chromosome Function. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3652-8_17
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