8OJ2

Crystal structure of the DNA binding domain of M. polymorpha Auxin Response Factor 2 (MpARF2) in complex with protomor-like sequence IR7

8OJ2 の概要

• エントリーDOI: 10.2210/pdb8oj2/pdb
• 分子名称: Auxin response factor, IR7, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (5 entities in total)
• 機能のキーワード: molecular caliper, auxin response factor, transcription factor, dna binding, nucleus, hormone response, transcription
• 由来する生物種: Marchantia polymorpha (liverwort); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47381.51

構造登録者

Crespo, I.,Weijers, D.,Boer, D.R. (登録日: 2023-03-23, 公開日: 2024-04-17, 最終更新日: 2025-04-23)

主引用文献

Crespo, I.,Malfois, M.,Rienstra, J.,Tarres-Sole, A.,van den Berg, W.,Weijers, D.,Boer, D.R.
The structure and function of the DNA binding domain of class B MpARF2 share more traits with class A AtARF5 than to that of class B AtARF1.
Structure, 2025

PubMed Abstract: Plant development is primarily controlled by the auxin phytohormones, which activate the auxin response factors (ARFs). Although the nuclear auxin pathway (NAP) is well studied, little is known on how ARFs specifically select target genes. Here, we investigated the DNA binding mechanism of ARF DNA binding domains (DBDs) from the activator class A and repressor class B in two evolutionary distant plant species, Marchantia polymorpha and Arabidopsis thaliana using fluorescence anisotropy, size exclusion chromatography, macromolecular crystallography (MX), and small-angle X-ray scattering (SAXS). We find that the previously proposed molecular caliper model, which partially explains the variability in binding of the ARFs to DNA, has been preserved throughout evolution. Our results show that the DBD of class B MpARF2 behaves more like class A AtARF5 than class B AtARF1. These findings suggest that DNA recognition of ARFs has diverged independently of the transcriptional output, which has significant implications for understanding diverse responses to auxin.

PubMed: 40086441
DOI: 10.1016/j.str.2025.02.006

実験手法

X-RAY DIFFRACTION (2.56 Å)