Zobrazeno 1 - 10
of 71
pro vyhledávání: '"Tomoya Tsukazaki"'
Autor:
Mai Ikei, Ryoji Miyazaki, Keigo Monden, Yusuke Naito, Azusa Takeuchi, Yutaro S Takahashi, Yoshiki Tanaka, Keina Murata, Takaharu Mori, Muneyoshi Ichikawa, Tomoya Tsukazaki
Publikováno v:
PLoS Biology, Vol 22, Iss 4, p e3002601 (2024)
Uptake of thiosulfate ions as an inorganic sulfur source from the environment is important for bacterial sulfur assimilation. Recently, a selective thiosulfate uptake pathway involving a membrane protein YeeE (TsuA) in Escherichia coli was characteri
Externí odkaz:
https://doaj.org/article/588485bb6b91481fb95d78913b6549c2
Autor:
Arata Furukawa, Kunihito Yoshikaie, Takaharu Mori, Hiroyuki Mori, Yusuke V. Morimoto, Yasunori Sugano, Shigehiro Iwaki, Tohru Minamino, Yuji Sugita, Yoshiki Tanaka, Tomoya Tsukazaki
Publikováno v:
Cell Reports, Vol 19, Iss 5, Pp 895-901 (2017)
Summary: Protein secretion mediated by SecYEG translocon and SecA ATPase is enhanced by membrane-embedded SecDF by using proton motive force. A previous structural study of SecDF indicated that it comprises 12 transmembrane helices that can conduct p
Externí odkaz:
https://doaj.org/article/48061d2fb26046939236aa25cee9ac83
Autor:
Yoshiki Tanaka, Yasunori Sugano, Mizuki Takemoto, Takaharu Mori, Arata Furukawa, Tsukasa Kusakizako, Kaoru Kumazaki, Ayako Kashima, Ryuichiro Ishitani, Yuji Sugita, Osamu Nureki, Tomoya Tsukazaki
Publikováno v:
Cell Reports, Vol 13, Iss 8, Pp 1561-1568 (2015)
The bacterial SecYEG translocon functions as a conserved protein-conducting channel. Conformational transitions of SecYEG allow protein translocation across the membrane without perturbation of membrane permeability. Here, we report the crystal struc
Externí odkaz:
https://doaj.org/article/459a478423c346838346f7051c7065f0
Publikováno v:
PLoS ONE, Vol 12, Iss 8, p e0183434 (2017)
In bacteria, the membrane protein complex SecY/E/G and SecA ATPase are essential for protein translocation. About 30% of newly synthesized proteins in the cytosol are targeted to and translocated across the cytoplasmic membrane by the Sec factors. Al
Externí odkaz:
https://doaj.org/article/98598dd0de294f358a6ab4a49492a8ab
Small single-strand DNA/RNA phages that infect gram-negative bacteria encode lysis proteins that induce cell lysis without directly degrading the cell wall. One such protein, the 37-residue LysMprotein derived from a lysis gene ofLevivirusphage M (ly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b734d5f512c5535f8e6c3de2c5492e18
https://doi.org/10.1101/2023.05.22.541694
https://doi.org/10.1101/2023.05.22.541694
Autor:
Hiroshi Inaba, Yurina Sueki, Muneyoshi Ichikawa, Arif Md. Rashedul Kabir, Takashi Iwasaki, Hideki Shigematsu, Akira Kakugo, Kazuki Sada, Tomoya Tsukazaki, Kazunori Matsuura
Publikováno v:
Science Advances. 8(36)
Microtubules play important roles in biological functions by forming superstructures, such as doublets and branched structures, in vivo. Despite the importance, it is challenging to construct these superstructures in vitro. Here, we designed a tetram
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f456508e3974cfbd798e8fb8cdb51e8
http://hdl.handle.net/10061/14799
http://hdl.handle.net/10061/14799
Publikováno v:
FEBS Letters. 595(14):1902-1913
A transporter of the multidrug and toxic compound extrusion (MATE) family, Nicotiana tabacum MATE2 (NtMATE2), is located in the vacuole membrane of the tobacco plant root and is involved in the transportation of nicotine, a secondary or specialized m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78f06b3d082f947864399ec456913ed6
http://hdl.handle.net/10061/14507
http://hdl.handle.net/10061/14507
Autor:
Tomoya Tsukazaki
Publikováno v:
The Protein Journal. 38(3):249-261
Protein translocation and membrane integration are fundamental, conserved processes. After or during ribosomal protein synthesis, precursor proteins containing an N-terminal signal sequence are directed to a conserved membrane protein complex called
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dd52f627b4f9dee46f7e3693df085e6
http://hdl.handle.net/10061/13375
http://hdl.handle.net/10061/13375
Autor:
Hironari Kamikubo, Shigehiro Iwaki, Yoshinori Akiyama, Yugo Hayashi, Yasushi Daimon, Tomoya Tsukazaki, Yoshiki Tanaka, Shintaro Nakayama, Mohammad Shahrizal, Shin-ichiro Narita
Publikováno v:
Journal of Molecular Biology. 431(3):625-635
The β-barrel assembly machinery (BAM) complex mediates the assembly of β-barrel membrane proteins in the outer membrane. BepA, formerly known as YfgC, interacts with the BAM complex and functions as a protease/chaperone for the enhancement of the a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d2f2ac481303e3e906cf75aa82f9db4
http://hdl.handle.net/10061/13292
http://hdl.handle.net/10061/13292
Autor:
Takamitsu Haruyama, Yasunori Sugano, Noriyuki Kodera, Hiroki Konno, Takayuki Uchihashi, Toshio Ando, Tomoya Tsukazaki, Yoshiki Tanaka
Publikováno v:
Structure. 27(1):152-160
Summary Membrane proteins play important roles in various cellular functions. To analyze membrane proteins, nanodisc technology using membrane scaffold proteins allows single membrane protein units to be embedded into the lipid bilayer disc without d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f0e05ece342f39c4b74ea1d5a67939f
http://hdl.handle.net/10061/13293
http://hdl.handle.net/10061/13293