Characterization of an alternative chromatin remodeling to parasperm in a cottid fish, Hemilepidotus gilberti

• Published in: Zoological science Vol. 28; no. 6; p. 438
• Main Authors: Nakauchi, Yuni, Hayakawa, Youichi, Fujinoki, Masakatsu, Yamamura, Orio, Kobayashi, Makito, Watanabe, Akihiko
• Format: Journal Article
• Language: English
• Published: Japan 01.06.2011
• Subjects: Amino Acid Sequence; Animals; Chromatin; Chromatin Assembly and Disassembly; Fishes - genetics; Fishes - physiology; Gene Expression Regulation - physiology; Male; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; Spermatozoa - physiology; Spermatozoa - ultrastructure
• ISSN: 0289-0003
• DOI: 10.2108/zsj.28.438

The dimorphic sperm of Hemilepidotus gilberti, i.e., haploid eusperm and diploid parasperm, have different morphologies corresponding to their own roles in fertilization. To estimate how these specific sperm morphologies were established, we focused on the nuclear morphologies and examined their changing processes in dimorphic spermiogenesis. Electron microscopic observation revealed that, in euspermatids, chromatin condensation first appeared as a mosaic pattern of moderate electrodense material in the peripheral region of the round nucleus. Those materials spread across the whole area to form a uniformly condensed nucleus. Chromatin condensation began similarly in paraspermatids to that in euspermatids. These became localized to one side of a nucleus and further condensed to form strong electrodense chromatin clusters, which are a specific feature of parasperm. From the remodeled nuclei of eusperm and parasperm, we found five and three kinds of sperm-specific basic proteins (SBPs), respectively, substituted to histones. The N-terminus amino acid sequences of the SBPs suggest that, in parasperm, one major SBP and two minor ones were distinct from each other. In eusperm nuclei, two kinds of specific SBPs were detected in addition to the homologs of parasperm SBPs. The specific SBPs had homologous amino acid sequences with huge arginine clusters, and one of them was most dominant among the five kinds of SBPs. The different combinations of SBPs in the eusperm and parasperm may cause a specific pattern of chromatin condensation in the dimorphic sperm nuclei of H. gilberti.