Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD

Kurzanzeige
dc.contributor.authorYudin, Denis
dc.contributor.authorJaskolowski, Mateusz
dc.contributor.authorFan, Ziyi
dc.contributor.authorBurg, Nicolas
dc.contributor.authorChandrasekar, Sowmya
dc.contributor.authorLentzsch, Alfred M.
dc.contributor.authorScaiola, Alain
dc.contributor.authorBothe, Adrian
dc.contributor.authorDeuerling, Elke
dc.contributor.authorGamerdinger, Martin
dc.contributor.authorShan, Shu-ou
dc.contributor.authorBan, Nenad
dc.date.accessioned2026-02-13T07:42:03Z
dc.date.available2026-02-13T07:42:03Z
dc.date.issued2025-12-19
dc.description.abstractThe replication-dependent histones H2A and H4 are among the most highly expressed proteins in eukaryotes during the S phase to ensure packaging of replicated chromosomes. Nearly all newly synthesized H2A and H4 are N-terminally acetylated by N-terminal acetyltransferase D (NatD) following excision of the initiator methionine by methionine aminopeptidases (MetAPs). These modifications influence chromatin function, but how they occur cotranslationally on these exceptionally abundant and small proteins was not understood. Here, we show that the nascent polypeptide-associated complex controls the cotranslational modification of histones H2A and H4 by recruiting NatD and the upstream enzyme MetAP1 to ribosomes. MetAP1 and NatD cooperate on the ribosome to create a confined environment for the efficient sequential modification of the nascent histone chain. Our work provides a mechanistic model for the early steps of histone maturation.
dc.description.versionpublisheddeu
dc.identifier.doi10.1126/sciadv.aeb1017
dc.identifier.ppn1962570843
dc.identifier.urihttps://kops.uni-konstanz.de/handle/123456789/76185
dc.language.isoeng
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dc.subject.ddc570
dc.titleMechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatDeng
dc.typeJOURNAL_ARTICLE
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kops.citation.bibtex
@article{Yudin2025-12-19Mecha-76185,
  title={Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD},
  year={2025},
  doi={10.1126/sciadv.aeb1017},
  number={51},
  volume={11},
  journal={Science Advances},
  author={Yudin, Denis and Jaskolowski, Mateusz and Fan, Ziyi and Burg, Nicolas and Chandrasekar, Sowmya and Lentzsch, Alfred M. and Scaiola, Alain and Bothe, Adrian and Deuerling, Elke and Gamerdinger, Martin and Shan, Shu-ou and Ban, Nenad},
  note={Article Number: eaeb1017}
}
kops.citation.iso690YUDIN, Denis, Mateusz JASKOLOWSKI, Ziyi FAN, Nicolas BURG, Sowmya CHANDRASEKAR, Alfred M. LENTZSCH, Alain SCAIOLA, Adrian BOTHE, Elke DEUERLING, Martin GAMERDINGER, Shu-ou SHAN, Nenad BAN, 2025. Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD. In: Science Advances. American Association for the Advancement of Science (AAAS). 2025, 11(51), eaeb1017. eISSN 2375-2548. Verfügbar unter: doi: 10.1126/sciadv.aeb1017deu
kops.citation.iso690YUDIN, Denis, Mateusz JASKOLOWSKI, Ziyi FAN, Nicolas BURG, Sowmya CHANDRASEKAR, Alfred M. LENTZSCH, Alain SCAIOLA, Adrian BOTHE, Elke DEUERLING, Martin GAMERDINGER, Shu-ou SHAN, Nenad BAN, 2025. Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD. In: Science Advances. American Association for the Advancement of Science (AAAS). 2025, 11(51), eaeb1017. eISSN 2375-2548. Available under: doi: 10.1126/sciadv.aeb1017eng
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