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Articles by Tomohito Yamada
Step-by-Step Maturation Mechanism of Binary Toxin Pore Revealed by Cryo-EM Analysis
Abstract Membrane pore-forming proteins (PFPs) form ring-shaped membrane-translocating oligomers on membranes, contributing to infection, immunity, and cell death functions. Binary toxins produced by some bacteria consist of an enzymatic component that acts as a toxin and a membrane-binding component that forms a pore that delivers the enzymatic component into target cells.
The expression of lignin biosynthesis genes during plant development and effects of downregulated cinnamyl alcohol dehydrogenase (CAD) gene in bahiagrass (Paspalum notatum Flügge)
Supporting Information Filename Description grs12419-sup-0001-Table_S1.docxWord 2007 document , 71 KB TABLE S1. List of primer sequences used in this study. grs12419-sup-0002-Fig_S1.docxWord 2007 document , 962.2 KB FIGURE S1. Alignment of caffeic acid O-methyltransferase (COMT) protein sequences of bahiagrass (Pn) and C4 plants, including Panicum virgatum (Pv), Sorghum bicolor (Pb), Soccharum officinarum (So) and Zea mays (Zm).
Future Changes in Tropical and Extratropical Cyclones Affecting Hokkaido and Their Related Precipitation Based on Large-Ensemble Climate Simulations
ProCite RefWorks Reference Manager BibTeX Zotero Adachi, S., and F.Kimura, 2007: A 36-year climatology of surface cyclogenesis in East Asia using high-resolution reanalysis data. SOLA, 3, 113–116, https://doi.org/10.2151/sola.2007-029. Adachi, S., and F. Kimura , 2007: A 36-year climatology of surface cyclogenesis in East Asia using high-resolution reanalysis data .
Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile - Nature Communications
Abstract Some bacteria express a binary toxin translocation system, consisting of an enzymatic subunit and translocation pore, that delivers enzymes into host cells through endocytosis. The most clinically important bacterium with such a system is Clostridioides difficile (formerly Clostridium). The CDTa and CDTb proteins from its system represent important therapeutic targets. CDTb has been proposed to be a di-heptamer, but its physiological heptameric structure has not yet been reported.
Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex
Abstract The iota toxin produced by Clostridium perfringens type E is a binary toxin comprising two independent polypeptides: Ia, an ADP-ribosyltransferase, and Ib, which is involved in cell binding and translocation of Ia across the cell membrane. Here we report cryo-EM structures of the translocation channel Ib-pore and its complex with Ia. The high-resolution Ib-pore structure demonstrates a similar structural framework to that of the catalytic ϕ-clamp of the anthrax protective antigen pore.
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