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The histone chaperone NASP maintains H3-H4 reservoirs in the early Drosophila embryo

ABSTRACT: Histones are essential for chromatin packaging and histone supply must be tightly regulated as excess histones are toxic. To drive the rapid cell cycles of the early embryo, however, excess histones are maternally deposited. Therefore, soluble histones must be buffered by histone chaperones but the chaperone necessary to stabilize soluble H3-H4 pools in the Drosophila embryo has yet to be identified. Here, we show that CG8223, the Drosophila ortholog of NASP, is a H3-H4-specific chaperone in the early embryo. NASP specifically binds to H3-H4 in the early embryo. We demonstrate that, while NASP is non-essential in Drosophila, NASP is maternal effect lethal gene. Embryos laid by NASP mutant mothers have a reduce rate of hatching and show defects in early embryogenesis. Critically, soluble H3-H4 pools are degraded in embryos laid by NASP mutant mothers. Our work identifies NASP as the critical H3-H4 histone chaperone in the Drosophila embryo.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

TISSUE(S): Embryo

SUBMITTER: Jonathan Davies

LAB HEAD: Jared T. Nordman

PROVIDER: PXD036809 | Pride | 2023-02-23

REPOSITORIES: Pride

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			Action	DRS
	JD-RT-001-HistoneFly-TMT16-20220716-TMT16--_1_.msf	Msf
	JD-RT-001-HistoneFly-TMT16-20220716-TMT16-0C_1.raw	Raw
	JD-RT-001-HistoneFly-TMT16-20220716-TMT16-100C_11.raw	Raw
	JD-RT-001-HistoneFly-TMT16-20220716-TMT16-10C_2.raw	Raw
	JD-RT-001-HistoneFly-TMT16-20220716-TMT16-20C_3.raw	Raw

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