Zobrazeno 1 - 10
of 91
pro vyhledávání: '"Miki Kinoshita"'
Autor:
Norihiro Takekawa, Tatsuro Nishikino, Jun-ichi Kishikawa, Mika Hirose, Miki Kinoshita, Seiji Kojima, Tohru Minamino, Takayuki Uchihashi, Takayuki Kato, Katsumi Imada, Michio Homma
Publikováno v:
mBio, Vol 15, Iss 10 (2024)
ABSTRACT The marine bacterium Vibrio alginolyticus possesses a polar flagellum driven by a sodium ion flow. The main components of the flagellar motor are the stator and rotor. The C-ring and MS-ring, which are composed of FliG and FliF, respectively
Externí odkaz:
https://doaj.org/article/f7945938f85b46149bd295709f42191c
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-12 (2024)
Abstract The flagellar type III secretion system (fT3SS) switches substrate specificity from rod-hook-type to filament-type upon hook completion, terminating hook assembly and initiating filament assembly. The C-terminal cytoplasmic domain of FlhA (F
Externí odkaz:
https://doaj.org/article/d74f9711a0f24b27bdb8f6c573d05d22
Autor:
Tsuyoshi Miki, Takeshi Uemura, Miki Kinoshita, Yuta Ami, Masahiro Ito, Nobuhiko Okada, Takemitsu Furuchi, Shin Kurihara, Takeshi Haneda, Tohru Minamino, Yun-Gi Kim
Publikováno v:
PLoS Biology, Vol 22, Iss 8, p e3002731 (2024)
Bacterial pathogens utilize the factors of their hosts to infect them, but which factors they exploit remain poorly defined. Here, we show that a pathogenic Salmonella enterica serovar Typhimurium (STm) exploits host polyamines for the functional exp
Externí odkaz:
https://doaj.org/article/9baf4b905c2347e297bfeedc4bcfa298
Publikováno v:
Biophysics and Physicobiology, Vol 19 (2022)
Bacteria employ the flagellar type III secretion system (fT3SS) to construct flagellum, which acts as a supramolecular motility machine. The fT3SS of Salmonella enterica serovar Typhimurium is composed of a transmembrane export gate complex and a cyt
Externí odkaz:
https://doaj.org/article/908a34ec28e54a37b8b2b87304655fd6
Autor:
Akihiro Kawamoto, Tomoko Miyata, Fumiaki Makino, Miki Kinoshita, Tohru Minamino, Katsumi Imada, Takayuki Kato, Keiichi Namba
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
The bacterial flagellar MS ring is a core transmembrane complex within the flagellar basal body. Here, cryoEM analysis suggests that the MS ring is formed by 34 full-length FliF subunits, with 23- and 11-fold subsymmetries in the inner and middle M r
Externí odkaz:
https://doaj.org/article/032d974f6e584299b453bf604e1b4f40
Autor:
Yumi Inoue, Miki Kinoshita, Mamoru Kida, Norihiro Takekawa, Keiichi Namba, Katsumi Imada, Tohru Minamino
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
Inoue and Kinoshita et al. report an important role for the flexible linker of the major flagellar export apparatus protein FlhA (FlhAL) in regulating the switch from secretion of hook-type to filament-type components. The data presented here improve
Externí odkaz:
https://doaj.org/article/1fbb7e21a75a444aa0d21c82f019586e
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
Kinoshita, Namba and Minamino show that a cluster of positively-charged arginines in the Salmonella FliI is necessary for formation of the FliI homo-hexamer ATPase. Through loss- and gain-of-function experiments, they demonstrate that hexamer assembl
Externí odkaz:
https://doaj.org/article/30c11a49b4e24a90a433cacebbad1062
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-11 (2021)
Minamino et al. report that the bacterial FlgN chaperone acts as a switch to activate a backup mechanism for H+-coupled flagellar protein export by interacting with FlhAC to activate the Na+-driven export engine. The proposed mechanism helps to expla
Externí odkaz:
https://doaj.org/article/de61e2e8ffbe45fdaa035216e7c70a89
Publikováno v:
Frontiers in Microbiology, Vol 13 (2022)
Most motile bacteria utilize the flagellar type III secretion system (fT3SS) to construct the flagellum, which is a supramolecular motility machine consisting of basal body rings and an axial structure. Each axial protein is translocated via the fT3S
Externí odkaz:
https://doaj.org/article/64fe284c672243c58dd29ae5c324bf15
Publikováno v:
Frontiers in Microbiology, Vol 12 (2021)
FlgN, FliS, and FliT are flagellar export chaperones specific for FlgK/FlgL, FliC, and FliD, respectively, which are essential component proteins for filament formation. These chaperones facilitate the docking of their cognate substrates to a transme
Externí odkaz:
https://doaj.org/article/99c72bb731634e7f8efa5208e0399db5