Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Mayuko Sakuma"'
Autor:
Norihiro Takekawa, Akihiro Kawamoto, Mayuko Sakuma, Takayuki Kato, Seiji Kojima, Miki Kinoshita, Tohru Minamino, Keiichi Namba, Michio Homma, Katsumi Imada
Publikováno v:
mBio, Vol 12, Iss 2 (2021)
The bacterial flagellum is a motility organelle formed by tens of thousands of protein molecules. At the earliest stage of flagellar assembly, a transmembrane protein, FliF, forms the MS-ring in the cytoplasmic membrane as the base for flagellar asse
Externí odkaz:
https://doaj.org/article/f5c71112b105479b824c20f8447b455b
Autor:
Norihiro Takekawa, Miyu Isumi, Hiroyuki Terashima, Shiwei Zhu, Yuuki Nishino, Mayuko Sakuma, Seiji Kojima, Michio Homma, Katsumi Imada
Publikováno v:
mBio, Vol 10, Iss 2 (2019)
ABSTRACT Many motile bacteria swim or swarm using a filamentous rotating organelle, the flagellum. FliL, a component protein of the flagellar motor, is known to enhance the motor performance under high-load conditions in some bacteria. Here we determ
Externí odkaz:
https://doaj.org/article/c1cb114bdb90420d873d81dea5accb51
Autor:
Katsumi Imada, Michio Homma, Norihiro Takekawa, Takayuki Kato, Mayuko Sakuma, Akihiro Kawamoto, Seiji Kojima, Keiichi Namba, Tohru Minamino, Miki Kinoshita
Publikováno v:
mBio
mBio, Vol 12, Iss 2 (2021)
mBio, Vol 12, Iss 2 (2021)
The bacterial flagellum is a motility organelle formed by tens of thousands of protein molecules. At the earliest stage of flagellar assembly, a transmembrane protein, FliF, forms the MS-ring in the cytoplasmic membrane as the base for flagellar asse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98aba8bd7c3d8196d5a9a89a81c07b5d
https://pubmed.ncbi.nlm.nih.gov/33653894
https://pubmed.ncbi.nlm.nih.gov/33653894
Autor:
Michio Homma, Norihiro Takekawa, Yuuki Nishino, Miyu Isumi, Shiwei Zhu, Katsumi Imada, Hiroyuki Terashima, Mayuko Sakuma, Seiji Kojima
Publikováno v:
mBio, Vol 10, Iss 2, p e00292-19 (2019)
mBio
mBio, Vol 10, Iss 2 (2019)
mBio
mBio, Vol 10, Iss 2 (2019)
Some flagellated bacteria regulate motor torque in response to the external load change. This behavior is critical for survival, but the mechanism has remained unknown. Here, we focused on a key protein, FliL of Vibrio alginolyticus, and solved the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8409ec4a8c199020bf0a019a680d896f
https://doaj.org/article/492e7c4b715d4d9aa295de2e2dd13664
https://doaj.org/article/492e7c4b715d4d9aa295de2e2dd13664
Autor:
Michio Homma, Satoshi Inaba, Takehiko Nishigaki, Seiji Kojima, Katsumi Imada, Shoji Nishikawa, Mayuko Sakuma
Publikováno v:
Journal of biochemistry. 166(2)
Bacteria have evolved various types of flagellum, an organella for bacterial motility, to adapt to their habitat environments. The number and the spatial arrangement of the flagellum are precisely controlled to optimize performance of each type of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51287308146ddd49e5d5268a78fbad1e
https://pubmed.ncbi.nlm.nih.gov/30989194
https://pubmed.ncbi.nlm.nih.gov/30989194
Autor:
Katsumi Imada, Seiji Kojima, Yuuki Nishino, Masato Takao, Mayuko Sakuma, Shiwei Zhu, Michio Homma, Na Li
Publikováno v:
Proceedings of the National Academy of Sciences. 111:13523-13528
The torque of the bacterial flagellum is generated by the rotor-stator interaction coupled with the ion flow through the channel in the stator. Anchoring the stator unit to the peptidoglycan layer with proper orientation around the rotor is believed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3c2dc0f04b6e6e89b17a5758a9f9538
https://doi.org/10.1073/pnas.1324201111
https://doi.org/10.1073/pnas.1324201111
Autor:
Yasuhiro Onoue, Yohei Miyanoiri, Michio Homma, Ananthanarayanan Kumar, Shiwei Zhu, Katsumi Imada, Seiji Kojima, Mayuko Sakuma, Miyu Isumi, Yuuki Nishino
Publikováno v:
Journal of biochemistry. 161(4)
The flagellar motor is embedded in the cell envelope and rotates upon interaction between the stator and the rotor. The rotation is powered by ion flow through the stator. A single transmembrane protein named FliL is associated with torque generation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71570a975caf70f818226934ed6144ae
https://pubmed.ncbi.nlm.nih.gov/28013221
https://pubmed.ncbi.nlm.nih.gov/28013221
Autor:
Masato Takao, Seiji Kojima, Chojiro Kojima, Michio Homma, Ikumi Kawahara, Mayuko Sakuma, Katsumi Imada, Gaby Almira
Publikováno v:
Structure. 26:590-598.e5
Summary The stator of the bacterial flagellar motor couples ion flow with torque generation. The ion-conducting stator channel opens only when incorporated into and anchored around the rotor via the peptidoglycan (PG) binding domain of the B subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56499f7d18fc5df7317d53e1e575d4da
https://doi.org/10.1016/j.str.2018.02.016
https://doi.org/10.1016/j.str.2018.02.016
Autor:
Katsumi Imada, Keiichi Namba, Akari Shinohara, Michio Homma, Seiji Kojima, Mayuko Sakuma, Toshiharu Yakushi
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:89-92
The polar flagellum of Vibrio alginolyticus is rotated by the sodium motor. The stator unit of the sodium motor consists of four different proteins: PomA, PomB, MotX and MotY. MotX and MotY, which are unique components of the sodium motor, form the T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::594e401e4ae89b897c946fd97ef3ef05
https://doi.org/10.1107/s1744309106055850
https://doi.org/10.1107/s1744309106055850
Autor:
Kenji Ogawa, Michio Homma, Yoshiyuki Okumura, Nobuo Yamashita, Katsumi Imada, Kei-ichi Uchiya, Toshiaki Nikai, Atsushi Hijikata, Mayuko Sakuma, Tsuyoshi Shirai
Publikováno v:
The Journal of biological chemistry. 288(24)
Elastase from Aspergillus sp. is an important factor for aspergillosis. AFUEI is an inhibitor of the elastase derived from Aspergillus fumigatus. AFUEI is a member of the I78 inhibitor family and has a high inhibitory activity against elastases of As
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99212758a7b37ffb8d88119a58b3c0bc
https://pubmed.ncbi.nlm.nih.gov/23640894
https://pubmed.ncbi.nlm.nih.gov/23640894