title: Histone H1 variants as sperm-specific nuclear proteins of Rana catesbeiana, and their role in maintaining a unique condensed state of sperm chromatin.
abstract: Amino acid analyses of nuclear basic proteins of an anuran amphibian, Rana catesbeiana, revealed that they are comprised of a full set of core histones and three types of lysine-rich, sperm-specific proteins. On the basis of their amino-acid compositions and partial amino-acid sequences of their trypsin-resistant cores, the sperm-specific proteins could be defined as members of the histone H1 family. Both micrococcal nuclease digestion and electron microscopy indicated that sperm chromatin consists of nucleosomal and fibrillar DNA structures which are irregularly interspersed with each other. When sperm nuclei were incubated with nucleoplasmin, nuclei decondensed to some extent, and the sperm-specific H1s were removed, but not completely. The residual sperm-specific histone H1 variants were also found in reconstituted male pronuclear chromatin, comprising regularly spaced nucleosomes. We conclude that sperm-specific histone H1 variants are essential for chromatin condensation in the sperm nuclei, but that their complete removal is not necessary for the remodeling into somatic chromatin that takes place after fertilization.
authors.affiliation: Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Itoh
authors.forename: J
authors.initials: J
authors.lastname: Ausio
authors.forename: C
authors.initials: C
authors.lastname: Katagiri
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002025:Bufonidae; D002467:Cell Nucleus / Q000737:chemistry* / Q000187:drug effects; D002843:Chromatin / Q000737:chemistry / Q000187:drug effects / Q000648:ultrastructure*; D006657:Histones / Q000145:classification / Q000235:genetics / Q000502:physiology*; D008297:Male; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000494:pharmacology; D056489:Nucleoplasmins; D009865:Oocytes; D010750:Phosphoproteins / Q000494:pharmacology; D011892:Rana catesbeiana / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013094:Spermatozoa / Q000737:chemistry* / Q000648:ultrastructure; D014357:Trypsin / Q000494:pharmacology; D014982:Xenopus laevis
chemical_list: D002843:Chromatin; D006657:Histones; D009687:Nuclear Proteins; D056489:Nucleoplasmins; D010750:Phosphoproteins; D014357:Trypsin