Publications by authors named "Hisako Ichihara"

Background: Plant genome information is fundamental to plant research and development. Along with the increase in the number of published plant genomes, there is a need for an efficient system to retrieve various kinds of genome-related information from many plant species across plant kingdoms. Various plant databases have been developed, but no public database covers both genomic and genetic resources over a wide range of plant species.

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A portal website that integrates a variety of information related to genomes of model and crop plants from databases (DBs) and the literature was generated. This website, named the Plant Genome DataBase Japan (PGDBj, http://pgdbj. jp/en/ ), is comprised of three component DBs and a cross-search engine which provides a seamless search over their contents.

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The Plant Genome DataBase Japan (PGDBj, http://pgdbj.jp/?ln=en) is a portal website that aims to integrate plant genome-related information from databases (DBs) and the literature. The PGDBj is comprised of three component DBs and a cross-search engine, which provides a seamless search over the contents of the DBs.

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Escherichia coli protein SixA was the first identified histidine protein phosphatase that dephosphorylates the histidine-containing phosphotransfer (HPt) domain of histidine kinase ArcB. The crystal structures of the free and tungstate-bound forms of SixA revealed an alpha/beta architecture with a fold unlike those previously described in eukaryotic protein phosphatases, but related to a family of phosphatases containing the arginine-histidine-glycine (RHG) motif at their active sites. Compared with these RHG phosphatases, SixA lacks an extra alpha-helical subdomain that forms a lid over the active site, thereby forming a relatively shallow groove important for accommodating the kidney-shaped four-helix bundle of the HPt domain.

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The sigma 28 kDa (sigma28) factor is a transcription factor specific for the expression of bacterial flagellar and chemotaxis genes. Its antisigma factor, FlgM, binds sigma28 factor and inhibits its activity as a transcription factor. In this study, crystals of the complex between Escherichia coli sigma28 and the C-terminal sigma28-binding region of FlgM were obtained.

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Competence-stimulating peptide (CSP) and ComD of the streptococcal species are a pheromone and its receptor, respectively, involved in the regulation of competence for natural genetic transformation. We show here that these molecules have undergone positive selection. This study is the first report of positive selection due to competition among bacterial populations.

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The members of the aquaporin family and those of the ClC chloride ion channel family consist of two-fold tandem repeats. The orientation of the N-terminal domain against membrane is opposite to that of the C-terminal domain. Several lines of evidence suggest that the extracellular and the cytoplasmic environments impose different evolutionary constraints on proteins (e.

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