TONSL histone H3.1 binding mechanism revealed as essential for DNA repair
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Research published in Science Advances shows that the DNA repair protein TONSL, also called TONSOKU, binds histone H3.1 through multiple pockets in its TPR domain, and that this binding is essential for DNA repair. The plant homolog TSK was found to preferentially bind H3.1 over the closely related H3.3. Two newly identified pockets cooperatively recognize two chemical marks on H3.1 — mono-methylation at lysine 4 and acetylation at lysine 27 — modifications associated with transcriptional regulatory elements such as enhancers and promoters. The work maps how TONSL is recruited to newly replicated chromatin, but how these recognition events integrate with downstream repair machinery remains an open question.
Written by a model from the reports · updated 3 hours ago
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- Science AdvancesPickTONSL/TONSOKU binding to histone H3.1 is required for DNA repair.
Research shows that TONSL/TONSOK binds histone H3.1 through multiple pockets in its TPR domain, and this binding is essential for DNA repair. Plant TSK preferentially binds H3.1 over its close homolog H3.3, and two newly identified pockets cooperate to recognize monomethylated K4 and acetylated K27 on H3.1, modifications associated with transcriptional regulatory elements such as enhancers and promoters.
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