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@ARTICLE{PulidoCorts:302837,
      author       = {L. Pulido-Cortés$^*$ and H. Gielingh and V. Thijssen and
                      M. Liu and R. Yoshisada and L. Romão Soares and S.
                      Nizamuddin$^*$ and F. Friedrich and H. Greschik$^*$ and L.
                      Peng$^*$ and R. Vargas Honorato and M. Jung$^*$ and A. M. J.
                      J. Bonvin and M. L. Biniossek and R. Schüle$^*$ and S.
                      Jongkees and H. van Ingen and H. T. M. Timmers$^*$},
      title        = {{M}olecular determinants for recognition of serotonylated
                      chromatin.},
      journal      = {Nucleic acids research},
      volume       = {53},
      number       = {13},
      issn         = {0305-1048},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {DKFZ-2025-01377},
      pages        = {gkaf612},
      year         = {2025},
      abstract     = {Post-translational modifications of histone tails
                      constitute a key epigenetic mechanism controlling chromatin
                      environment and gene transcription. Serotonylation of
                      histone H3Q5 (H3Q5ser) is a recently discovered mark
                      associated with active transcription of RNA polymerase II
                      (pol II)-transcribed genes. The direct link between H3Q5ser
                      and the pol II transcription machinery relies on the TFIID
                      subunit TAF3. The presence of H3Q5ser enhances TAF3 binding
                      to H3K4me3, but the molecular determinants underlying this
                      interaction remained unclear. Here, we resolve the binding
                      mode of TAF3-PHD to H3K4me3Q5ser identifying a novel binding
                      surface for H3Q5ser using solution nuclear magnetic
                      resonance spectroscopy. This reveals how H3Q5ser recognizes
                      a conserved surface of the TAF3-PHD via CH-π interactions
                      in an edge-face conformation involving a proline residue
                      stabilized by a tryptophan. This combination of proline and
                      tryptophan is unique to the PHD finger of TAF3 and conserved
                      among TAF3 orthologues. Our findings establish a framework
                      for the molecular recognition of serotonylated chromatin,
                      laying the foundation for developing epigenetic inhibitors
                      targeting serotonylation-dependent transcriptional
                      regulation in neuronal development.},
      keywords     = {Chromatin: metabolism / Chromatin: chemistry / Chromatin:
                      genetics / Histones: metabolism / Histones: chemistry /
                      Histones: genetics / Transcription Factor TFIID: chemistry /
                      Transcription Factor TFIID: metabolism / Transcription
                      Factor TFIID: genetics / TATA-Binding Protein Associated
                      Factors: chemistry / TATA-Binding Protein Associated
                      Factors: metabolism / TATA-Binding Protein Associated
                      Factors: genetics / Humans / Protein Binding / Protein
                      Processing, Post-Translational / Models, Molecular /
                      Epigenesis, Genetic / Binding Sites / RNA Polymerase II:
                      metabolism / RNA Polymerase II: genetics / Histone
                      Acetyltransferases / Chromatin (NLM Chemicals) / Histones
                      (NLM Chemicals) / Transcription Factor TFIID (NLM Chemicals)
                      / TATA-Binding Protein Associated Factors (NLM Chemicals) /
                      TATA-binding protein associated factor 250 kDa (NLM
                      Chemicals) / RNA Polymerase II (NLM Chemicals) / Histone
                      Acetyltransferases (NLM Chemicals)},
      cin          = {FR01},
      ddc          = {570},
      cid          = {I:(DE-He78)FR01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40637225},
      pmc          = {pmc:PMC12238850},
      doi          = {10.1093/nar/gkaf612},
      url          = {https://inrepo02.dkfz.de/record/302837},
}