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Magori, Shimpei*; Kira, Erika*; Shibata, Satoshi*; Umehara, Yosuke*; Kochi, Hiroshi*; Hase, Yoshihiro; Tanaka, Atsushi; Sato, Shusei*; Tabata, Satoshi*; Kawaguchi, Masayoshi*
Molecular Plant-Microbe Interactions, 22(3), p.259 - 268, 2009/03
Times Cited Count:101 Percentile:92.67(Biochemistry & Molecular Biology)Legume plants tightly control the development and number of symbiotic root nodules. In , this regulation required
in the shoots, suggesting that a long-distance communication between the shoots and the roots may exist. To better understand its molecular basis, we isolated and characterized a novel hypernodulating mutant of
named
(
). Reciprocal grafting with wild type showed that
hypernodulation is determined by the root genotype. Moreover, grafting a
shoot onto a
rootstock did not exhibit any obvious additive effects on the nodule number. These observations indicate that a shoot factor
and a root factor
participate in the same genetic pathway which governs the long-distance signaling of nodule number control.
may function downstream of
and the gene product
might serve as a receptor or mediator of unknown mobile signal molecules that are transported from the shoots to the roots.
Yoshikawa, Hiroshi; Sakaki, Hironao; Sako, Hiroyuki; Takahashi, Hiroki; Shen, G.; Kato, Yuko; Ito, Yuichi; Ikeda, Hiroshi*; Ishiyama, Tatsuya*; Tsuchiya, Hitoshi*; et al.
Proceedings of International Conference on Accelerator and Large Experimental Physics Control Systems (ICALEPCS '07) (CD-ROM), p.62 - 64, 2007/10
J-PARC is a large scale facility of the proton accelerators for the multi-purpose of scientific researches in Japan. This facility consists of three accelerators and three experimental stations. Now, J-PARC is under construction, and LINAC is operated for one year, 3GeV synchrotron has just started the commissioning in this October the 1st. The completion of this facility will be next summer. The control system of accelerators established fundamental performance for the initial commissioning. The most important requirement to the control system of this facility is to minimize the activation of accelerator devices. In this paper, we show that the performances of each layer of this control system have been achieved in the initial stage.
Sato, Daisuke*; Mori, Mari*; Katayama, Hisato*; Kitamura, Harushige*; Kawai, Toshihiko*; Fujimaki, Shu; Suzui, Nobuo; Kawachi, Naoki; Ishii, Satomi; Matsuhashi, Shimpei; et al.
JAEA-Review 2006-042, JAEA Takasaki Annual Report 2005, P. 128, 2007/02
no abstracts in English
Ozawa, Akira*; Matsuta, Kensaku*; Nagatomo, Takashi*; Mihara, Mototsugu*; Yamada, Kazunari*; Yamaguchi, Takayuki*; Otsubo, Takashi*; Momota, Sadao*; Izumikawa, Takuji*; Sumikama, Toshiyuki*; et al.
Physical Review C, 74(2), p.021301_1 - 021301_4, 2006/08
Times Cited Count:41 Percentile:88.8(Physics, Nuclear)no abstracts in English
Yonezawa, Yasushige*; Tanaka, Shimpei*; Kubota, Tomomi*; Wakabayashi, Katsuzo*; Yutani, Katsuhide*; Fujiwara, Satoru
Journal of Molecular Biology, 323(2), p.237 - 251, 2002/10
Times Cited Count:74 Percentile:74.76(Biochemistry & Molecular Biology)It is known that hen egg white lysozyme (HEWL) forms amyloid fibrils in highly concentrated ethanol solutions. In order to gain an insight into the mechanism of the amyloid fibril formation, the structures of HEWL in solutions of various protein and ethanol concentrations were investigated with small-angle X-ray and neutron scattering. It was shown that the structural states of HEWL were distinguished as the monomer state, the state of the dimer formation, the state of the protofilament formation, the protofilament state, and the state towards the formation of the amyloid fibrils. Circular dichroism measurements showed that the large changes in the secondary structures of HEWL occurred during the dimer formation. Structural characterization showed that the dimers had an elongated shape, the protofilaments were formed by stacking of the dimers with their long axis (nearly) perpendicular to the protofilament axis, and the changes of the structural states towards the amyloid fibril formation occurred via lateral association of the protofilaments.