Histone variant H3.3 residue S31 is essential for Xenopus gastrulation regardless of the deposition pathway
In: Nature Communications ; volume 11, issue 1 ; ISSN 2041-1723, 2020
Online
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Zugriff:
Vertebrates exhibit specific requirements for replicative H3 and non-replicative H3.3 variants during development. To disentangle whether this involves distinct modes of deposition or unique functions once incorporated into chromatin, we combined studies in Xenopus early development with chromatin assays. Here we investigate the extent to which H3.3 mutated at residues that differ from H3.2 rescue developmental defects caused by H3.3 depletion. Regardless of the deposition pathway, only variants at residue 31—a serine that can become phosphorylated—failed to rescue endogenous H3.3 depletion. Although an alanine substitution fails to rescue H3.3 depletion, a phospho-mimic aspartate residue at position 31 rescues H3.3 function. To explore mechanisms involving H3.3 S31 phosphorylation, we identified factors attracted or repulsed by the presence of aspartate at position 31, along with modifications on neighboring residues. We propose that serine 31-phosphorylated H3.3 acts as a signaling module that stimulates the acetylation of K27, providing a chromatin state permissive to the embryonic development program.
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Histone variant H3.3 residue S31 is essential for Xenopus gastrulation regardless of the deposition pathway
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Autor/in / Beteiligte Person: | Sitbon, David ; Boyarchuk, Ekaterina ; Dingli, Florent ; Loew, Damarys ; Almouzni, Geneviève ; Université de Recherche Paris Sciences et Lettres ; Agence Nationale de la Recherche |
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Zeitschrift: | Nature Communications ; volume 11, issue 1 ; ISSN 2041-1723, 2020 |
Veröffentlichung: | Springer Science and Business Media LLC, 2020 |
Medientyp: | academicJournal |
DOI: | 10.1038/s41467-020-15084-4 |
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