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Histone variant H2A.L.2 guides transition protein - dependent protamine assembly in male germ cells

ABSTRACT: Histone replacement by small basic proteins, transition proteins (TPs) and protamines (Prms) constitutes an essential step for the successful production of male gametes, yet nothing is known on the underlying functional interplay between histones, TPs and Prms. By studying spermatogenesis in the absence of H2A.L.2, a spermatid-specific histone variant, we identify a new step essential for the "metamorphosis" of nucleosomes to nucleoprotamines. H2A.L.2 plays the role of a "Trojan horse" histone, which induces dramatic structural changes that enables the invasion of nucleosomes by TPs, themselves driving the processing and incorporation of Prms. H2A.L.2 incorporation initiates a series of rapidly changing transitional states that ultimately shift to a more stable state characterized by nucleoprotamine assembly and histone-TP Powered by Editorial Manager® and ProduXion Manager® from Aries Systems Corporationdisplacement, leading to the generation of mature spermatozoa. The textbook view of histone-to-nucleoprotein transition needs to be revisited to include a new step with H2A.L.2 assembly prior to the action of TPs and Prms.

ORGANISM(S): Mus musculus

PROVIDER: GSE93251 | GEO | 2017/05/10

SECONDARY ACCESSION(S): PRJNA360424

REPOSITORIES: GEO

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Project description:Specialized chromatin containing CENP-A nucleosomes instead of H3 nucleosomes is found at all centromeres. However, the mechanisms that specify the locations at which CENP-A chromatin is assembled remain elusive in organisms with regional, epigenetically regulated centromeres. It is known that normal centromeric DNA is transcribed in several systems including the fission yeast, Schizosaccharomyces pombe. Here, we show that factors which preserve stable histone H3 chromatin during transcription also play a role in preventing promiscuous CENP-A(Cnp1) deposition in fission yeast. Mutations in the histone chaperone FACT impair the maintenance of H3 chromatin on transcribed regions and promote widespread CENP-A(Cnp1) incorporation at non-centromeric sites. FACT has little or no effect on CENP-A(Cnp1) assembly at endogenous centromeres where CENP-A(Cnp1) is normally assembled. In contrast, Clr6 complex II (Clr6-CII; equivalent to Rpd3S) histone deacetylase function has a more subtle impact on the stability of transcribed H3 chromatin and acts to prevent the ectopic accumulation of CENP-A(Cnp1) at specific loci, including subtelomeric regions, where CENP-A(Cnp1) is preferentially assembled. Moreover, defective Clr6-CII function allows the de novo assembly of CENP-A(Cnp1) chromatin on centromeric DNA, bypassing the normal requirement for heterochromatin. Thus, our analyses show that alterations in the process of chromatin assembly during transcription can destabilize H3 nucleosomes and thereby allow CENP-A(Cnp1) to assemble in its place. We propose that normal centromeres provide a specific chromatin context that limits reassembly of H3 chromatin during transcription and thereby promotes the establishment of CENP-A(Cnp1) chromatin and associated kinetochores. These findings have important implications for genetic and epigenetic processes involved in centromere specification. In total, 24 samples: 22 ChIP DNA files (10 different conditions), 2 Input files.

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Histone variant H2A.L.2 guides transition protein - dependent protamine assembly in male germ cells

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