ArticleEpigenetics & chromatin2025
The linker histone chaperone Prothymosin α (PTMA) is essential for efficient DNA damage repair and the recruitment of PARP1.
Article in Epigenetics & chromatin, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Targeting Leukopoiesis: Pharmacological and Biotechnological Strategies for the Treatment of Leukopenia.Biomedicines · 2026Review
- Time-Resolved Single-Molecule FRET Reveals Length-Dependent Nucleosome Decompaction by Poly(ADP-ribose).bioRxiv : the preprint server for biology · 2026Article
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4 authors.
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Abstract
backgroundMammalian cells have numerous DNA repair pathways to repair lesions generated by replication errors, metabolism, and exogenous agents. Cells can sense and respond to DNA damage within seconds, suggesting that there is a highly effective sensor of lesions although the mechanistic details are unclear. The DNA damage response in mammalian cells results in a localized transient de-condensation of chromatin, loss of linker histones and the recruitment of DNA repair proteins such as PARP1 and chromatin remodelers.
resultsHere we investigated the interactions between poly(ADP-ribose) polymerase-1 (PARP1), the linker histone H1.0 and linker histone chaperone Prothymosin α (PTMA). Using H1.0 tagged with a photoconvertible fluorescent protein, we observed a significant increase in the initial rate of exit of H1.0 from regions of chromatin containing microirradiation-induced DNA lesions. Surprisingly, this was also seen in Parp1
conclusionWe suggest that DNA damage alters the interaction of H1.0 with the nucleosome to allow the chaperone PTMA to bind and promote release of linker histones thereby initiating the local chromatin de-condensation necessary for the efficient recruitment of repair proteins such as PARP1. In this context linker histones may serve as in situ "sensors" of DNA damage.
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