Protamines from liverwort are produced by post-translational cleavage and C-terminal di-aminopropanelation of several male germ-specific H1 histones




D'Ippolito, Robert Anthony
Minamino, Naoki
Rivera-Casas, Ciro
Cheema, Manjinder S.
Bai, Dina L.
Kasinsky, Harold E.
Shabanowitz, Jeffrey
Eirin-Lopez, Jose M.
Ueda, Takashi
Hunt, Donald F.

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Journal of Biological Chemistry


Protamines are small, highly-specialized, arginine-rich, and intrinsically-disordered chromosomal proteins that replace histones during spermiogenesis in many organisms. Previous evidence supports the notion that, in the animal kingdom, these proteins have evolved from a primitive replication-independent histone H1 involved in terminal cell differentiation. Nevertheless, a direct connection between the two families of chromatin proteins is missing. Here, we primarily used electron transfer dissociation MS-based analyses, revealing that the protamines in the sperm of the liverwort Marchantia polymorpha result from post-translational cleavage of three precursor H1 histones. Moreover, we show that the mature protamines are further post-translationally modified by di-aminopropanelation, and previous studies have reported that they condense spermatid chromatin through a process consisting of liquid-phase assembly likely involving spinodal decomposition. Taken together, our results reveal that the interesting evolutionary ancestry of protamines begins with histone H1 in both the animal and plant kingdoms.



14-3-3 protein, mass spectrometry (MS), histone, electron microscopy (EM), chromatography, di-aminopropanelation, histone H1, Marchantia, mass spectrometry, protamines


D’Ippolito, R. A., Minamino, N., Rivera-Casas, C., Cheema, M. S., Bai, D. L., Kasinsky, H. E., … Ausió, J. (2019). Protamines from liverwort are produced by post -translational cleavage and C-terminal di-aminopropanelation of several male germ-specific H1 histones. Journal of Biological Chemistry, 294(44), 16364-16373.