%0 Journal Article
%A Delaforge, Elise
%A Due, Amanda D
%A Theisen, Frederik Friis
%A Morffy, Nicolas
%A O’Shea, Charlotte
%A Blackledge, Martin
%A Strader, Lucia C
%A Skriver, Karen
%A Kragelund, Birthe B
%T Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation
%J Nucleic acids symposium series
%V 53
%N 4
%@ 0305-1048
%C Oxford
%I Oxford Univ. Press
%M PUBDB-2025-01383
%P gkaf065
%D 2025
%Z ISSN 1362-4962 not unique: **2 hits**.
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:001417619200001
%R 10.1093/nar/gkaf065
%U https://bib-pubdb1.desy.de/record/626391