Solution Structure of the Major DNA-binding Domain of Arabidopsis thaliana Ethylene-insensitive3-like3
pmid: 15811366
Solution Structure of the Major DNA-binding Domain of Arabidopsis thaliana Ethylene-insensitive3-like3
Ethylene-insensitive3 (EIN3) and EIN3-like (EIL) proteins are essential transcription factors in the ethylene signaling of higher plants. The EIN3/EIL proteins bind to the promoter regions of the downstream genes and regulate their expression. The location of the DNA-binding domain (DBD) in the primary structure was unclear, since the proteins show no sequence similarity to other known DBDs. Here, we identify the major DBD of an EIN3/EIL protein, Arabidopsis thaliana EIL3, containing a key mutational site for DNA binding and signaling (ein3-3 site), and determine its solution structure by NMR spectroscopy. The structure consists of five alpha-helices, possessing a novel fold dissimilar to known DBD structures. By a chemical-shift perturbation analysis, a region including the ein3-3 site is suggested to be involved in DNA binding.
Models, Molecular, Proline, Arabidopsis Proteins, Molecular Sequence Data, Arabidopsis, Nuclear Proteins, DNA, Surface Plasmon Resonance, Protein Structure, Tertiary, DNA-Binding Proteins, Structural Homology, Protein, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment, Transcription Factors
Models, Molecular, Proline, Arabidopsis Proteins, Molecular Sequence Data, Arabidopsis, Nuclear Proteins, DNA, Surface Plasmon Resonance, Protein Structure, Tertiary, DNA-Binding Proteins, Structural Homology, Protein, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment, Transcription Factors
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