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Protamines: Structural Complexity, Evolution and Chromatin Patterning

[ Vol. 18 , Issue. 8 ]

Author(s):

Harold E. Kasinsky, Jose Maria Eirin-Lopez and Juan Ausio   Pages 755 - 771 ( 17 )

Abstract:


Despite their relatively arginine-rich composition, protamines exhibit a high degree of structural variation. Indeed, the primary structure of these histone H1-related sperm nuclear basic proteins (SNBPs) is not random and is the depository of important phylogenetic information. This appears to be the result of their fast rate of evolution driven by positive selection. The way by which the protein variability participates in the transitions that lead to the final highly condensed chromatin organization of spermatozoa at the end of spermiogenesis is not clearly understood. In this paper we focus on the transient chromatin/nucleoplasm patterning that occurs in either a lamellar step or an inversion step during early and mid-spermiogenesis. This takes place in a small subset of protamines in internally fertilizing species of vertebrates, invertebrates and plants. It involves “complex” protamines that are processed, replaced, or undergo side chain modification (such as phosphorylation or disulfide bond formation) during the histone-to-protamine transition. Characteristic features of such patterning, as observed in TEM photomicrographs, include: constancy of the dominant pattern repeat distance λm despite dynamic changes in developmental morphology, bicontinuity of chromatin and nucleoplasm, and chromatin orientation either perpendicular or parallel to the nuclear envelope. This supports the hypothesis that liquid - liquid phase separation by the mechanism of spinodal decomposition may be occurring during spermiogenesis in these species. Spinodal decomposition involves long wave fluctuations of the local concentration with a low energy barrier and thus differs from the mechanism of nucleation and growth that is known to occur during spermiogenesis in internally fertilizing mammals.

Keywords:

Protamines, structure, evolution, chromatin/nucleoplasm patterning, lamellae, spermiogenesis, sperm nuclear basic proteins, LAMELLAR, spinodal decomposition, protamine SNBP type, HISTONE H1, ARGININE-RICH PROTAMINES, structural heterogeneity, phylogeny, SPERMATIDS, genome, keratinous protamines, thermal quenching, nucleation, PatchProtamines, structure, evolution, chromatin/nucleoplasm patterning, lamellae, spermiogenesis, sperm nuclear basic proteins, LAMELLAR, spinodal decomposition, protamine SNBP type, HISTONE H1, ARGININE-RICH PROTAMINES, structural heterogeneity, phylogeny, SPERMATIDS, genome, keratinous protamines, thermal quenching, nucleation, Patch

Affiliation:

University of Victoria Department of Biochemistry, Petch Bldg., Room 258, Victoria, BC, V8W 3P6,Canada.



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