Yokoyama. T.*, Miyazaki, R., Suzuki, T., Dohmae, N., Nagai, H., Tsukazaki, T., Kubori, T.*, Akiyama, Y.* (2025).
Cleavage cascade of the sigma regulator FecR orchestrates TonB-dependent signal transduction. Proc. Natl. Acad. Sci. U. S. A., 122, 16, e2500366122. DOI : 10.1073/pnas.2500366122
京都大学HP 細菌が環境中の鉄の存在を「知る」しくみを解明 膜タンパク質の多段階切断を介して、細胞外の情報が細胞内へ伝達される
2024年
Watanabe, A., Koyano, F., Imai, K., Hizukuri, Y., Ogiwara, S., Ito, T., Miyamoto, J., Shibuya, C., Kimura, M., Toriumi, K., Motono, C., Arai, M., Tanaka, K., Akiyama, Y., Yamano, K., Matsuda, N.* (2024).
The origin of esterase activity of Parkinson’s disease causative factor DJ-1 implied by evolutionary trace analysis of its prokaryotic homolog HchA. J. Biol. Chem., 300, 107476. DOI : 10.1016/j.jbc.2024.107476
Ikeda, Y., Miyazaki, R., Tsukazaki, T., Akiyama, Y., and Mori, H.* (2024).
Translation arrest cancellation of VemP, a secretion monitor in Vibrio, is regulated by multiple cis and trans factors, including SecY. J. Biol. Chem., 300, 107735. DOI : 10.1016/j.jbc.2024.107735
2023年
Yokoyama, T., Yamagata, Y., Honna, S., Mizuno, S., Katagiri, S., Oi, R., Nogi, T., Hizukuri, Y.*, and Akiyama, Y.* (2023).
S2P intramembrane protease RseP degrades small membrane proteins and suppresses the cytotoxicity of intrinsic toxin HokB. mBio, 14, e0108623. DOI : 10.1128/mbio.01086-23
2022年
Miyazaki, R., Ai, M.a, Tanaka, N. a, Suzuki, T., Dhomae, N., Tsukazaki, T., Akiyama, Y., and Mori, H.* (2022). aequally contributed
Inner membrane YfgM–PpiD heterodimer acts as a functional unit that associates with the SecY/E/G translocon and promotes protein translocation. J. Biol. Chem., 298, 102572. DOI : 10.1016/j.jbc.2022.102572
Imaizumi, Y.a, Takanuki, K.a, Miyake, T.a, Takemoto, M., Hirata, K., Hirose, M., Oi, R., Kobayashi, T., Miyoshi, K., Aruga, R., Yokoyama, T., Katagiri, S., Matsuura, H., Iwasaki, K., Kato, K., Kaneko, M. K., Kato, Y., Tajiri, M., Akashi, S., Nureki, N., Hizukuri, Y.*, Akiyama, Y.*, and Nogi, T.* (2022). aequally contributed
Mechanistic insights into intramembrane proteolysis by E. coli site-2 protease homolog RseP. Sci. Adv., 8(34), eabp9011. DOI : 10.1126/sciadv.abp9011
京都大学HP 細胞膜の中ではたらく特殊なタンパク質分解酵素の構造を解明~細菌感染症の新たな治療法の開発へ期待~
Qiao, Z., Yokoyama, T., Yan, X., Beh, I., Shi, J., Basak, S., Akiyama, Y.*, and Gao, Y.* (2022).
Cryo-EM structure of the entire FtsH-HflKC AAA protease complex. Cell Rep., 39, 110890. DOI : 10.1016/j.celrep.2022.110890
2021年
Miyazaki, R., Watanabe, T., Yoshitani, K., and Akiyama, Y.* (2021).
Edge-strand of BepA interacts with immature LptD on the β-barrel assembly machine to direct it to on- and off-pathways. eLife, 10:e70541. DOI : 10.7554/eLife.70541
Yokoyama, T., Niinae, T., Tsumagari, K., Imami, K., Ishihama, Y., Hizukuri, Y.*, and Akiyama, Y.* (2021).
The Escherichia coli S2P intramembrane protease RseP regulates ferric citrate uptake by cleaving the sigma factor regulator FecR. J. Biol. Chem., 296, 100673. DOI : 10.1016/j.jbc.2021.100673
Tamura-Sakaguchi, R., Aruga, R., Hirose, M., Ekimoto, T., Miyake, T., Hizukuri, Y., Oi, R., Kaneko, M. M., Kato, Y., Akiyama, Y., Ikeguchi, M., Iwasaki, K., and Nogi, T.* (2021).
Moving toward generalizable NZ-1 labeling for 3D structure determination with optimized epitope tag insertion. Acta Crystallogr. D Struct. Biol., 77, 645-662. DOI : 10.1107/S2059798321002527
京都大学HP タンパク質の抗体ラベリング技術を改良し、構造解析をアシスト -電子顕微鏡やX線結晶解析による構造決定を加速化-
2020年
Miyazaki, R., Akiyama, Y., and Mori, H.* (2020).
Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation. eLife, 9, e62623. DOI : 10.7554/eLife.62623
Miyake, T., Hizukuri, Y.*, and Akiyama, Y*. (2020).
Involvement of a membrane-bound amphiphilic helix in substrate discrimination and binding by an Escherichia coli S2P peptidase RseP. Front. Microbiol., 11, 607381. DOI : 10.3389/fmicb.2020.607381
Daimon, Y.a, Narita, S.a, Miyazaki, R., Hizukuri, Y., Mori, H., Tanaka, Y., Tsukazaki, T., and Akiyama, Y.* (2020). aequally contributed
Reversible auto-inhibitory regulation of Escherichia coli metallopeptidase BepA for selective β-barrel protein degradation. Proc. Natl. Acad. Sci. U. S. A. 117, (45) 27989-27996. DOI : 10.1073/pnas.2010301117