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@ARTICLE{Delaforge:626391,
      author       = {Delaforge, Elise and Due, Amanda D and Theisen, Frederik
                      Friis and Morffy, Nicolas and O’Shea, Charlotte and
                      Blackledge, Martin and Strader, Lucia C and Skriver, Karen
                      and Kragelund, Birthe B},
      title        = {{A}llovalent scavenging of activation domains in the
                      transcription factor {ANAC}013 gears transcriptional
                      regulation},
      journal      = {Nucleic acids symposium series},
      volume       = {53},
      number       = {4},
      issn         = {0305-1048},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2025-01383},
      pages        = {gkaf065},
      year         = {2025},
      note         = {ISSN 1362-4962 not unique: **2 hits**.},
      abstract     = {Transcriptional regulation involves interactions between
                      transcription factors, coregulators, and DNA. Intrinsic
                      disorder is a major player in this regulation, but
                      mechanisms driven by disorder remain elusive. Here, we
                      address molecular communication within the stress-regulating
                      Arabidopsis thaliana transcription factor ANAC013. Through
                      high-throughput screening of ANAC013 for transcriptional
                      activation activity, we identify three activation domains
                      within its C-terminal intrinsically disordered region. Two
                      of these overlap with acidic islands and form dynamic
                      interactions with the DNA-binding domain and are released,
                      not only upon binding of target promoter DNA, but also by
                      nonspecific DNA. We show that independently of DNA binding,
                      the RST (RCD--SRO--TAF4) domain of the negative regulator
                      RCD1 (Radical-induced Cell Death1) scavenges the two acidic
                      activation domains positioned vis-à-vis through allovalent
                      binding, leading to dynamic occupation at enhanced affinity.
                      We propose an allovalency model for transcriptional
                      regulation, where sequentially close activation domains in
                      both DNA-bound and DNA-free states allow for efficient
                      regulation. The model is likely relevant for many
                      transcription factor systems, explaining the functional
                      advantage of carrying sequentially close activation
                      domains.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:001417619200001},
      doi          = {10.1093/nar/gkaf065},
      url          = {https://bib-pubdb1.desy.de/record/626391},
}