Structural Studies on Molecular Recognition of Nucleic Acid Bases

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Purification, characterization and crystallization of sigma factors, sigma28, sigma38, and sigma70, were performed. Measurements of fluorescent polarization and surface plasmon resonance showed that sigma28 and sigma38 could bind to promoter DNAs, especially strongly to the-10 region of the promoters. Crystals of sigma38 were obtained by a vapor-diffusion method. Crystal structure of a yeast transcription factor PHO4 complexed with DNA was solved by the conventional MIR method. The crystal structure revealed how PHO4 recognizes the DNA sequence at an atomic resolution. Crystals of a murine transcription factor IRF-2 complexed with DNA and a yeast transcription factor papl bound to DNA also were obtained. Structure determination of these crystals are underway. Crystal structure of a HPt (histidine-containing phosphotransfer) domain of E.coli sensor protein ArcB was solved. The crystal structure indicated that the domain exists both in prokaryote and eukaryote.