6QEC

DNA binding domain of LUX ARRYTHMO in complex with DNA

6QEC の概要

• エントリーDOI: 10.2210/pdb6qec/pdb
• 関連するPDBエントリー: 5LXU
• 分子名称: DNA (5'-D(*AP*TP*TP*CP*GP*AP*AP*TP*AP*T*TP*AP*TP*AP*TP*TP*CP*GP*AP*A)-3'), Transcription factor LUX, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: protein-dna complex myb domain, circadian clock protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 13863.31

構造登録者

Zubieta, C.,Nayak, A. (登録日: 2019-01-07, 公開日: 2020-02-05, 最終更新日: 2024-01-24)

主引用文献

Silva, C.S.,Nayak, A.,Lai, X.,Hutin, S.,Hugouvieux, V.,Jung, J.H.,Lopez-Vidriero, I.,Franco-Zorrilla, J.M.,Panigrahi, K.C.S.,Nanao, M.H.,Wigge, P.A.,Zubieta, C.
Molecular mechanisms of Evening Complex activity inArabidopsis.
Proc.Natl.Acad.Sci.USA, 117:6901-6909, 2020

PubMed Abstract: The Evening Complex (EC), composed of the DNA binding protein LUX ARRHYTHMO (LUX) and two additional proteins EARLY FLOWERING 3 (ELF3) and ELF4, is a transcriptional repressor complex and a core component of the plant circadian clock. In addition to maintaining oscillations in clock gene expression, the EC also participates in temperature and light entrainment, acting as an important environmental sensor and conveying this information to growth and developmental pathways. However, the molecular basis for EC DNA binding specificity and temperature-dependent activity were not known. Here, we solved the structure of the DNA binding domain of LUX in complex with DNA. Residues critical for high-affinity binding and direct base readout were determined and tested via site-directed mutagenesis in vitro and in vivo. Using extensive in vitro DNA binding assays of LUX alone and in complex with ELF3 and ELF4, we demonstrate that, while LUX alone binds DNA with high affinity, the LUX-ELF3 complex is a relatively poor binder of DNA. ELF4 restores binding to the complex. In vitro, the full EC is able to act as a direct thermosensor, with stronger DNA binding at 4 °C and weaker binding at 27 °C. In addition, an excess of ELF4 is able to restore EC binding even at 27 °C. Taken together, these data suggest that ELF4 is a key modulator of thermosensitive EC activity.

PubMed: 32165537
DOI: 10.1073/pnas.1920972117

実験手法

X-RAY DIFFRACTION (1.9 Å)