Molecular structure of chromatin during sperm differentiation of the dogfish Scyliorhinus caniculus (L.).
The molecular structure of chromatin during dogfish spermiogenesis was examined by electron microscopy after the dispersion of nuclei at low ionic strength. In early and late stages of differentiation (round and elongating spermatids), chromatin is globular, although basic nuclear proteins are different from those present in somatic nuclei. Three protein fractions are complexed with DNA in sperm nuclei. These fractions appear at the end of differentiation (elongated spermatids), subsequently undergoing a modification of their solubilization properties; only one protein fraction remains acid-soluble. Dispersed chromatin from sperm nuclei again shows a beads-on-a-string configuration both in the presence of the three specific sperm proteins and when the acid soluble fraction is extracted. Variations of the mean diameter of chromatin subunits during spermiogenesis appear rather limited compared to extensive modifications of chromatin superstructures.
D000818:Animals; D002843:Chromatin / Q000648:ultrastructure*; D002868:Chromosomal Proteins, Non-Histone; D004247:DNA; D004284:Dogfish / Q000502:physiology*; D006657:Histones; D008297:Male; D008854:Microscopy, Electron; D008968:Molecular Conformation; D009690:Nucleic Acid Conformation; D011479:Protamines; D011487:Protein Conformation; D012754:Sharks / Q000502:physiology*; D013091:Spermatogenesis
D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D011479:Protamines; D004247:DNA