Organization and Evolution of the Protamine Genes of Salmonid Fishes

  • Gordon H. Dixon
  • Judd M. Aiken
  • Jacek M. Jankowski
  • Deborah I. Mckenzie
  • R. Moir
  • J. Christopher States
Part of the NATO ASI Series book series (NSSA, volume 101)


In the final stages of development of the male gametes of almost all animals and some plants, new sperm-specific basic proteins are synthesized and form complexes with the DNA. This process, which is a characteristic feature of male gametogenesis, is frequently, but not always, accompanied by a replacement of the pre-existing, somatic histones by the new sperm proteins and very often correlates with a profound re-organization of the chromatin involving the formation of a highly-condensed and transcriptionally-inactive sperm nucleus. The variety of sperm basic proteins is extremely wide and the distribution of different types through phylogeny, apparently quite irregular. This is in strong contrast with the somatic histones which are amongst the proteins most strongly conserved in evolution. In 1969, Bloch (1), compiled a catalogue of sperm histones and in Figure 1, a classification based on the one suggested by Bloch is presented. There are four broad categories of sperm basic proteins classified in order of their increasing degree of difference from the somatic histones. They are as follows: (a) Histone-like proteins whose amino-acid composition and electrophoretic behavior are very similar to the somatic histones, and which are found in some Echinoderms (2), some Anuran amphibia and some fishes, e.g. Carpio; (b) Intermediate proteins which are clearly different in composition (often being more arginine-rich) and electrophoretic mobility, and which are seen in some Echinoderms, some mollusks, some amphibia, and some fishes; (c) True protamines which are very arginine-rich, often quite small, and which are seen in some mollusks, amphibia, fishes (particularly Salmonids and Clupeids), reptiles, birds, and metatherian mammals; (d) Stable protamines or basic keratins, which are somewhat longer polypeptides that, in addition to being arginine-rich, also contain ∿ 6–9 residues of 1/2-cystine; they occur in some insects, an amphibian, and all eutherian mammals. The presence of the high content of 1/2-cystine confers great mechanical and chemical stability to the sperm nuclei since a three-dimensional network of disulfide bridges is formed which can only be disrupted in vitro by thiols in the presence of strong denaturing agents (3–5). There is, in addition, another class of sperm proteins found in the very unusual ameboid sperm of crabs and crayfish (Arthropoda), which have nuclei in which the chromatin is less condensed than in somatic cells. These proteins of ameboid sperm are not basic but acidic in nature (5, 6) and have not been extensively characterized.


Rainbow Trout Histone Gene Sperm Protein Pacific Herring Protamine Gene 
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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Gordon H. Dixon
    • 1
  • Judd M. Aiken
    • 1
  • Jacek M. Jankowski
    • 1
  • Deborah I. Mckenzie
    • 1
  • R. Moir
    • 1
  • J. Christopher States
    • 1
  1. 1.Department of Medical Biochemistry Faculty of Medicine Health Sciences CentreUniversity of CalgaryCalgaryCanada

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