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Nat Commun March 9, 2020; 11 (1): 1256.
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Histone variant H3.3 residue S31 is essential for Xenopus gastrulation regardless of the deposition pathway.

Sitbon D , Boyarchuk E , Dingli F , Loew D , Almouzni G .

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.

PubMed ID: 32152320
PMC ID: PMC7062693
Article link: Nat Commun

Species referenced: Xenopus laevis
Genes referenced: abl1 arhgef5 daxx hira
GO keywords: chromatin
Morpholinos: h3-3a MO3

Article Images: [+] show captions
References [+] :
Ahmad, Histone H3 variants specify modes of chromatin assembly. 2003, Pubmed