Solution structure of the B3 DNA binding domain of the Arabidopsis cold-responsive transcription factor RAV1

• Published in: The Plant cell Vol. 16; no. 12; pp. 3448 - 3459
• Main Authors: Yamasaki, K, Kigawa, T, Inoue, M, Tateno, M, Yamasaki, T, Yabuki, T, Aoki, M, Seki, E, Matsuda, T, Tomo, Y
• Format: Journal Article
• Language: English
• Published: England American Society of Plant Biologists 01.12.2004
• Subjects: Acclimatization - physiology; Amino Acid Sequence - physiology; Amino acids; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Arabidopsis thaliana; Auxins; binding sites; Binding Sites - genetics; Chemical equilibrium; Cold Temperature; Deoxyribonucleases, Type II Site-Specific - chemistry; Deoxyribonucleases, Type II Site-Specific - metabolism; DNA; DNA - metabolism; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Enzymes; Evolution, Molecular; Hydrogen bonds; Models, Molecular; Molecular Conformation; Molecules; nuclear magnetic resonance spectroscopy; Nuclear Magnetic Resonance, Biomolecular; Phylogeny; Plant cells; protein secondary structure; Protein Structure, Secondary - physiology; Protein Structure, Tertiary - genetics; Proteins; Sequence Homology, Amino Acid; Transcription factors
• ISSN: 1040-4651; 1532-298X; 1532-298X
• DOI: 10.1105/tpc.104.026112

The B3 DNA binding domain is shared amongst various plant-specific transcription factors, including factors involved in auxin-regulated and abscisic acid-regulated transcription. Herein, we report the NMR solution structure of the B3 domain of the Arabidopsis thaliana cold-responsive transcription factor RAV1. The structure consists of a seven-stranded open beta-barrel and two alpha-helices located at the ends of the barrel and is significantly similar to the structure of the noncatalytic DNA binding domain of the restriction enzyme EcoRII. An NMR titration experiment revealed a DNA recognition interface that enabled us to propose a structural model of the protein-DNA complex. The locations of the DNA-contacting residues are also likely to be similar to those of the EcoRII DNA binding domain.