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

ABSTRACT: 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.

SUBMITTER: D'Ippolito RA

PROVIDER: S-EPMC6827293 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Epigenetic marking of sperm by post-translational modification of histones and protamines.

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Histone H1 and the origin of protamines.

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H1 histones control the epigenetic landscape by local chromatin compaction.

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Role of H1 linker histones in mammalian development and stem cell differentiation.

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Project description: Not available

| S-EPMC4375056 | biostudies-literature

Novel nucleosomal particles containing core histones and linker DNA but no histone H1.

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