Journal Article

PUBDB-2025-01383

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation

Delaforge, E. ; Due, A. D. ; Theisen, F. F. ; Morffy, N. ; O’Shea, C. ; Blackledge, M. ; Strader, L. C. ; Skriver, K. (Corresponding author) ; Kragelund, B. B. (Corresponding author)

2025
Oxford Univ. Press Oxford

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Please use a persistent id in citations: doi:10.1093/nar/gkaf065  doi:10.3204/PUBDB-2025-01383

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.

Note: ISSN 1362-4962 not unique: **2 hits**.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2025

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