Papers
Number of the published data : 80
No. Publishing type Authorship Title Author Journal Publisher Volume/issue/page Publication date ISSN DOI URL Summary
1 Research paper (scientific journal)

Structural basis of the binding affinity of Mlp24p and Mlp37p for various amino acids
Y. Takahashi, S. Nishiyama, I. Kawagishi, K. Imada
Biochemical and Biophysical Research Communications
Elsevier
523, 233-238
2020/02/26

10.1016/j.bbrc.2019.12.055


2 Research paper (scientific journal)
Joint
High pressure inhibits signaling protein binding to the flagellar motor and bacterial chemotaxis through enhanced hydration.
Hata, H., Nishihara, Y., Nishiyama, M., Sowa, Y., Kawagishi, I., & Kitao, A.
Scientific Reports
Springer Nature Limited
10, 2351
2020/02/11

10.1038/s41598-020-59172-3


3 Research paper (scientific journal)
Joint
Calcium ions modulate amino acid sensing of the chemoreceptor Mlp24 of Vibrio cholerae.
Takahashi, Y., Nishiyama, S., Sumita, K., Kawagishi, I., & Imada, K.
Journal of Bacteriology
The American Society for Microbiology
201, e00779-18
2019/04/09

10.1128/JB.00779-18


4 Research paper (scientific journal)
Joint
The dimerization site-2 of the bacterial DNA-binding protein H-NS is required for gene silencing and stiffened nucleoprotein filament formation.
Yamanaka, Y., Winardhi, R. S., Yamauchi, E., Nishiyama, S. I., Sowa, Y., Yan, J., Kawagishi, I., Ishihama, A. & Yamamoto, K.
Journal of Biological Chemistry
The American Society for Biochemistry and Molecular Biology
293, 9496-9505
2018/04/25

10.1074/jbc.RA117.001425


5 Research paper (scientific journal)
Joint
Chemotactic behaviors of Vibrio cholerae cells.
Kawagishi, I. & Nishiyama, S.
Minamino, T. & Namba, K. (eds.) The Bacterial Flagellum: Methods and Protocols, Methods in Molecular Biology
Springer Science+Business Media
1593, 259-271
2017/05/07
1940-6029
10.1007/978-1-4939-6927-2_21

Vibrio cholerae, the causative agent of cholera, swims in aqueous environments with a single polar flagellum. In a spatial gradient of a chemical, the bacterium can migrate in “favorable” directions, a property that is termed chemotaxis. The chemotaxis of V. cholerae is not only critical for survival in various environments and but also is implicated in pathogenicity. In this chapter, we describe how to characterize the chemotactic behaviors of V. cholerae: these methods include swarm assay, temporal stimulation assay, capillary assay, and receptor methylation assay.
6 Research paper (scientific journal)
Joint
Substrate-dependent dynamics of the multidrug efflux transporter AcrB of Escherichia coli
Kentaro Yamamoto, Rei Tamai, Megumi Yamazaki, Takehiko Inaba, Yoshiyuki Sowa & Ikuro Kawagishi
Scientific Reports

6, 21909-NA
2016/02/26

10.1038/srep21909.

The resistance-nodulation-cell division (RND)-type xenobiotic efflux system plays a major role in the multidrug resistance of gram-negative bacteria. The only constitutively expressed RND system of Escherichia coli consists of the inner membrane transporter AcrB, the membrane fusion protein AcrA, and the outer membrane channel TolC. The latter two components are shared with another RND-type transporter AcrD, whose expression is induced by environmental stimuli. Here, we demonstrate how RND-type ternary complexes, which span two membranes and the cell wall, form in vivo. Total internal reflection fluorescence (TIRF) microscopy revealed that most fluorescent foci formed by AcrB fused to green fluorescent protein (GFP) were stationary in the presence of TolC but showed lateral displacements when tolC was deleted. The fraction of stationary AcrB-GFP foci decreased with increasing levels of AcrD. We propose that the AcrB-containing complex becomes unstable upon the induction of AcrD, which presumably replaces AcrB, a process we call "transporter exchange." This instability is suppressed by AcrB-specific substrates, suggesting that the ternary complex is stabilised when it is in action. These results suggest that the assembly of the RND-type efflux system is dynamically regulated in response to external stimuli, shedding new light on the adaptive antibiotic resistance of bacteria.
7 Research paper (scientific journal)
Joint
Identification of a Vibrio cholerae chemoreceptor that senses taurine and amino acids as attractants
So-ichiro Nishiyama, Yohei Takahashi, Kentaro Yamamoto, Daisuke Suzuki, Yasuaki Itoh, Kazumasa Sumita, Yumiko Uchida, Michio Homma, Katsumi Imada & Ikuro Kawagishi
Scientific Reports

6, 20866-NA
2016/02/16

10.1038/srep20866

Vibrio cholerae, the etiological agent of cholera, was found to be attracted by taurine (2-aminoethanesulfonic acid), a major constituent of human bile. Mlp37, the closest homolog of the previously identified amino acid chemoreceptor Mlp24, was found to mediate taxis to taurine as well as L-serine, L-alanine, L-arginine, and other amino acids. Methylation of Mlp37 was enhanced upon the addition of taurine and amino acids. Isothermal titration calorimetry demonstrated that a purified periplasmic fragment of Mlp37 binds directly to taurine, L-serine, L-alanine and L-arginine. Crystal structures of the periplamic domain of Mlp37 revealed that L-serine and taurine bind to the membrane-distal PAS domain in essentially in the same way. The structural information was supported by characterising the in vivo properties of alanine-substituted mutant forms of Mlp37. The fact that the ligand-binding domain of the L-serine complex had a small opening, which would accommodate a larger R group, accounts for the broad ligand specificity of Mlp37 and allowed us to visualise ligand binding to Mlp37 with fluorescently labelled L-serine. Taken together, we conclude that Mlp37 serves as the major chemoreceptor for taurine and various amino acids.
8 Research paper (scientific journal)
Joint
Liquid-based iterative recombineering method tolerant to counter-selection escapes
Tominaga, M., Kawai-Noma, S., Kawagishi, I., Sowa, Y., Saito, K., Umeno, D.
PLoS One

10, e0119818
2015

10.1371/journal.pone.0119818

Selection-based recombineering is a flexible and proven technology to precisely modify bacterial genomes at single base resolution. It consists of two steps of homologous recombination followed by selection/counter-selection. However, the shortage of efficient counter-selectable markers limits the throughput of this method. Additionally, the emergence of 'selection escapees' can affect recombinant pools generated through this method, and they must be manually removed at each step of selection-based recombineering. Here, we report a series of efforts to improve the throughput and robustness of selection-based recombineering and to achieve seamless and automatable genome engineering. Using the nucleoside kinase activity of herpes simplex virus thymidine kinase (hsvTK) on the non-natural nucleoside dP, a highly efficient, rapid, and liquid-based counter-selection system was established. By duplicating hsvtk gene, combined with careful control of the population size for the subsequent round, we effectively eliminated selection escapes, enabling seamless and multiple insertions/replacement of gene-size fragments in the chromosome. Four rounds of recombineering could thus be completed in 10 days, requiring only liquid handling and without any need for colony isolation or genotype confirmation. The simplicity and robustness of our method make it broadly accessible for multi-locus chromosomal modifications.
9 Research paper (scientific journal)
Joint
A putative porin gene of Burkholderia sp. NK8 involved in chemotaxis toward β-ketoadipate
Yamamoto-Tamura, K., Kawagishi, I., Ogawa, N., Fujii, T.
Bioscience, Biotechnology, and Biochemistry

79
2015

10.1080/09168451.2015.1006571

Burkholderia sp. NK8 can utilize 3-chlorobenzoate (3CB) as a sole source of carbon because it has a megaplasmid (pNK8) that carries the gene cluster (tfdT-CDEF) encoding chlorocatechol-degrading enzymes. The expression of tfdT-CDEF is induced by 3CB. In this study, we found that NK8 cells were attracted to 3CB and its degradation products, 3- and 4-chlorocatechol, and β-ketoadipate. Capillary assays revealed that a pNK8-eliminated strain (NK82) was defective in chemotaxis toward β-ketoadipate. The introduction of a plasmid carrying a putative outer membrane porin gene, which we name ompNK8, into strain NK82 restored chemotaxis toward β-ketoadipate. RT-PCR analyses demonstrated that the transcription of the ompNK8 gene was enhanced in the presence of 3CB.
10 Research paper (scientific journal)
Joint
Hypoxia-induced localization of chemotaxis-related signaling proteins in Vibrio cholerae
Hiremath, G., Hyakutake, A., Yamamoto, K., Ebisawa, T., Nakamura, T., Nishiyama, S., Homma, M., Kawagishi, I.
Molecular Microbiology

95, 780-790
2015

10.1111/mmi.12887

Vibrio cholerae has three sets of chemotaxis-related signaling proteins, of which only System II has been shown to be involved in chemotaxis. Here we examined localization of green fluorescent protein (GFP)-fused components of System I. The histidine kinase (CheA1) and the adaptor (CheW0) of System I localized to polar and lateral membrane regions when incubated with standing incubation (microaerobic conditions), but their localization was lost after shaking (aerobic conditions). A transmembrane receptor of System I also showed polar and lateral localization with standing incubation. By contrast, GFP-fused components of System II localized constitutively to the flagellated pole. Nitrogen gas, sodium azide or carbonylcyanide m-chlorophenylhydrazone induced localization of CheA1-GFP even with shaking incubation, suggesting that the localization is controlled in response to changes in energy metabolism. Fluorescently labeled tetracysteine-tagged CheA1 also showed azide-induced localization, arguing against artifactual effects of GFP fusions. These results suggest that System I components are assembled into the supramolecular signaling complex in response to reduced cellular energy states, raising the possibility that the System I complex plays a role in sensing and signaling under microaerobic environments, such as in the host intestine.
11 (MISC) Introduction and explanation (scientific journal)
Joint
Polymodal sensing by bacterial chemoreceptors
So-ichiro Nishiyama, Hirotaka Tajima and Ikuro Kawagishi
J. Antibact. Antifung. Agents.

41, 35-43
2013



地球上のさまざまな場所に生育する細菌は大きな環境変化(光,熱,酸素,栄養状態など)に晒されることが多く,その変化を敏感・迅速に察知し,的確に応答する必要がある。栄養物質に近づき,有害物質から遠ざかる走化性は,そのような環境応答の一種である。興味深いことに,走化性に関わる受容体(走化性受容体)は,複数の化学物質を認識するとともに,温度やpHなどの変化も受容する多機能なセンサーとして働く。本稿では,大腸菌およびコレラ菌走化性受容体の構造と刺激認識のメカニズムに焦点を合わせて紹介する。
12 (MISC) Introduction and explanation (scientific journal)
Joint
Molecular mechanism of bacterial chemotaxis and its regulation
Kimiko Yamamoto-Tamura, So-ichiro Nishiyama, and Ikuro Kawagishi
Antibiotics & Chemotherapy

29, 91-99
2013



病原細菌は,宿主への侵入・感染・病徴発現に適した環境を感知し,病原性因子の生産や新たな宿主への伝搬に必要な状態へと自らの生理機能を切り替える。二成分制御系はこのような環境シグナルの感知と応答のシステムで,運動性細菌の走化性においても中心的な役割を果たす。細菌は栄養物質・有害な物質を特異的な受容体で感知し,二成分制御系を介してそのシグナルをべん毛や線毛に伝え,より生存に適した場所へ移動できる。本稿ではコレラ菌を中心に,走化性応答のメカニズムと病原性やバイオフィルム形成との関わりについて概説する。
13 Research paper (scientific journal)
Joint
Mlp24 (McpX) of Vibrio cholerae implicated in pathogenicity functions as a chemoreceptor for multiple amino acids
Nishiyama, N., Suzuki, D., Itoh, Y., Suzuki, K., Tajima, H., Hyakutake, A., Homma. M., Butler-Wu. S. M., Camilli, A., and Kawagishi, I.
Infection and Immunity

80, 3170-3178
2012

10.1128/IAI.00039-12

The chemotaxis of Vibrio cholerae, the causative agent of cholera, has been implicated in pathogenicity. The bacterium has more than forty genes for methyl-accepting chemotaxis protein (MCP)-like proteins (MLPs). Here we found that glycine and at least 18 L-amino acids, including serine, arginine, asparagine and proline, serve as attractants to the classical biotype strain O395N1. Based on the sequence comparison with V. parahaemolyticus, we speculated that at least 17 MLPs of V. cholerae may mediate chemotactic responses. Among them, Mlp24 (previoeusly named McpX) is required for the production of cholera toxin upon mouse infection. The mlp24-deletion strains of both classical and El Tor biotypes showed defects in taxis toward several amino acids, which were complemented by the expression of Mlp24. These amino acids enhanced methylation of Mlp24. Serine, arginine, asparagine and proline were shown to bind directly to the periplasmic fragment of Mlp24. The structural information of its closest homolog Mlp37 predicts that Mlp24 has two potential ligand-binding pockets per subunit, the membrane-distal of which was suggested, by mutational analyses, to be involved in sensing of amino acids. These results suggest that Mlp24 is a chemoreceptor for multiple amino acids, including serine, arginine and asparagine, which were previously shown to stimulate the expression of several virulence factors, implying that taxis toward a set of amino acids play critical roles in pathogenicity of V. cholerae.
14 Research paper (scientific journal)
Joint
Ligand specificity determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar
Tajima, H., Imada, K., Sakuma, M., Hattori, F., Nara, T., Kamo, N., Homma, M. & Kawagishi, I.
Journal of Biological Chemistry

286, 42200-42210
2011

10.1074/jbc.M111.221887

Escherichia coli has closely related amino acid chemoreceptors with distinct ligand specificity: Tar for L-aspartate and Tsr for L-serine. Crystallography of the ligand-binding domain of Tar identified the residues interacting with aspartate, most of which are conserved in Tsr. However, swapping of the non-conserved residues between Tsr and Tar did not change ligand specificity. Analyses with chimeric receptors led us to hypothesize that distinct three-dimensional arrangements of the conserved ligand-binding residues are responsible for ligand specificity. To test this hypothesis, the structures of the apo and serine-binding forms of the ligand-binding domain of Tsr were determined at 1.95 and 2.5 Å resolutions, respectively. Some of the Tsr residues are arranged differently from the corresponding aspartate-binding residues of Tar to form a high-affinity serine-binding pocket. The ligand-binding pocket of Tsr was surrounded by negatively charged residues, which presumably exclude negatively charged aspartate molecules. We propose that all these Tsr- and Tar-specific features contribute to specific recognition of serine and aspartate with the arrangement of the side chain of residue 68 (Asn in Tsr and Ser in Tar) being most critical.
15 (MISC) Introduction and explanation (scientific journal)
Joint
Phototactic and chemotactic signal transduction by transmembrane receptors and transducers in microorganisms
Suzuki, D., Irieda, H., Homma, M., Kawagishi, I., and Sudo, Y.
Sensor

10, 4010-4039
2010




16 Research paper (scientific journal)
Joint
Thermosensing function of the Escherichia coli redox sensor Aer
Nishiyama, N., Ohno, S., Ohta, N., Inoue, Y., Fukuoka, F., Ishijima, A., and Kawagishi, I.
Journal of Bacteriology

192, 1740-1743
2010



Some motile bacteria can sense temperature and move to temperatures best-suited to growth. This behavior, called thermotaxis, has been extensively studied in Escherichia coli. Our early studies revealed that E. coli thermotaxis is mediated by chemoreceptors that also sense amino acids or sugars: Tsr (serine), Tar (aspartate and maltose) and Trg (ribose and galactose) function as warm sensors, producing counter-clockwise or clockwise flagellar rotation signals upon temperature upshift and downshift, respectively. Tap (dipeptides, pyrimidines) functions as a cold sensor, producing CW and CCW signals upon temperature increases and decreases, respectively. Unique among these temperature sensors, Tar switches from a warm sensor to a cold sensor after adaptation to its ligand, aspartate. Intensive studies of Tar revealed that the receptor’s transmembrane and methylation domains play important roles in thermotactic responses, but what part of the chemoreceptor molecule actually senses temperature remains unknown. In this study, we found that the aerotaxis transducer Aer also has temperature-sensing ability. An otherwise receptor-less strain expressing only aer showed extremely smooth swimming and did not show any thermoresponse. However, after imposing a CW rotational bias by adding two distinct repellents, the cells showed CCW and CW responses to temperature upshifts and downshifts, respectively. We also observed similar thermoresponse mediated by a CW-biased mutant Aer without repellents. These results suggest that Aer functions as a warm sensor, even though, unlike the Tar, Tap, Tsr, and Trg chemoreceptors, Aer does not have a periplasmic ligand-binding domain. Thus, temperature sensing by E. coli chemoreceptors may be a general attribute of their highly-conserved cytoplasmic signaling domain (or their less conserved transmembrane domain).
17 Research paper (scientific journal)
Joint
Systematic Cys mutagenesis of FlgI, the flagellar P-ring component of Escherichia coli
Hizukuri, Y., Kojima, S., Yakushi, T., Kawagishi, I., and Homma, M.
Microbiology

154, 810-817
2008




18 Research paper (scientific journal)
Joint
The bidirectional polar and unidirectional lateral flagellar motors of Vibrio alginolyticus are controlled by a single CheY species
Kojima, M., Kubo, R., Yakushi, T., Homma, M., and Kawagishi, I.
Molecular Microbiology

64, 57-67
2007



The bacterial flagellar motor is an elaborate molecular machine converting ion-motive force into mechanical force (rotation). One of its remarkable feature is its instantaneous switching, without changing the direction of ion flow, of rotational sense or speed upon binding of the response regulator CheY, which causes a change in swimming mode to achieve chemotaxis. Vibrio alginolyticus has dual flagellar systems, the Na+-driven polar flagellum (Pof) and the H+-driven lateral flagella (Laf), that are used for swimming in liquid and swarming over surfaces, respectively. Here we showed that both swimming and surface swarming of V. alginolyticus involve chemotaxis and are regulated by a single CheY species. Some of the mutations of the CheY residues conserved among various bacteria had different effects on the Pof and Laf motors, implying that CheY acts differently on the two motors. Furthermore, analyses of tethered cells revealed that their switching modes are different: the Laf motor rotates exclusively in counterclockwise and is slowed down by CheY, whereas the Pof motor is bidirectional and CheY controls its rotational sense. This is the first report that a single CheY species can exert two distinct motor switching rotations.
19 Research paper (scientific journal)
Joint
Involvement of minor components associated with the FimA fimbriae of Porphyromonas gingivalis in adhesive functions
Nishiyama, S., Murakami, Y., Nagata, H., Shizukuishi, S., Kawagishi, I., and Yoshimura, F.
Microbiology

153, 1916-1925
2007




20 Research paper (scientific journal)
Joint
The voltage-gated Na+ channel NaVBP co-localizes with methyl-accepting chemotaxis protein at cell poles of alkaliphilic Bacillus pseudofirmus OF4
Fujinami, S., Sato, T., Trimmer, J. S., Spiller, B. W., Clapham, D. E., Krulwich, T. A., Kawagishi, I., and Ito, M.
Microbiology

153, 4027-4038
2007




21 Research paper (scientific journal)
Joint
Helical distribution of the bacterial chemoreceptor via co-localization with the Sec protein translocation machinery
Shiomi, D., Yoshimoto, M., Homma, M., and Kawagishi, I.
Molecular Microbiology

60, 894-906
2006



In Escherichia coli, chemoreceptor clustering at a cell pole seems critical for signal amplification and adaptation. However, little is known about the mechanism of localization itself. Here we examined whether the aspartate chemoreceptor (Tar) is inserted directly into the polar membrane by using its fusion to green fluorescent protein (GFP). After induction of Tar-GFP, fluorescent spots first appeared in lateral membrane regions, and later cell poles became predominantly fluorescent. Unexpectedly, Tar-GFP showed a helical arrangement in lateral regions, which was more apparent when a Tar-GFP derivative with two cysteine residues in the periplasmic domain were crosslinked to form higher oligomers. Moreover, similar distribution was observed even when the cytoplasmic domain of the double cysteine Tar-GFP mutant was replaced by that of the kinase EnvZ, which does not localize to a pole. Observation of GFP-SecE and a translocation-defective MalE-GFP mutant, as well as indirect immunofluorescence microscopy on SecG, suggested that the general protein translocation machinery (Sec) itself is arranged into a helical array, with which Tar is transiently associated. The Sec coil appeared distinct from the MreB coil, an actin-like cytoskeleton. These findings will shed new light on the mechanisms underlying spatial organization of membrane proteins in E. coli.
22 Research paper (scientific journal)
Joint
The role of the intramolecular disulfide bond in FlgI, the flagellar P-ring component of Escherichia coli
Hizukuri, Y., Yakushi, T., Kawagishi, I., and Homma, M.
Journal of Bacteriology

188, 4190-4197
2006




23 Research paper (scientific journal)
Joint
Differential recognition of citrate and a metal-citrate complex by the bacterial chemoreceptor Tcp
Iwama, T., Ito, Y., Aoki, H., Sakamoto, H., Yamagata, S., Kawai, K., and Kawagishi, I.
Journal of Biological Chemistry

281, 17727-17735
2006



The chemoreceptor Tcp of Salmonella enterica serovar Typhimurium can sense citrate and a metal-citrate complex as distinct attractants. In this study, we tried to investigate the molecular mechanism of this discrimination. That citrate binds directly to Tcp was verified by the site-specific thiol modification assays using membrane fractions prepared from E. coli cells expressing the mutant Tcp receptors in which single Cys residues were introduced at positions in the putative ligand-binding pocket. To determine the region responsible for the ligand discrimination, we screened for mutations defective in taxis to magnesium in the presence of citrate. All of the isolated mutants from random mutagenesis with hydroxylamine were defective both in citrate- and metal-citrate-sensing and the mutated residues are located in or near the α1-α2 and α3-α4 loops within the periplasmic domain. Further analyses with site-directed replacements around these regions demonstrated that the residue Asn67, which is presumed to lie at the subunit interface of the Tcp homodimer, plays a critical role in the recognition of the metal-citrate complex but not that of citrate. Various amino acids at this position differentially affect the citrate- and metal-citrate-sensing abilities. Thus, for the first time, the abilities to sense the two attractants were genetically dissected. Based on the results obtained in this study, we propose models, in which the discrimination of the metal-citrate complex from citrate involves cooperative interaction at Asn67 and allosteric switching.
24 Research paper (scientific journal)
Joint
Control of chemotactic signal gain via modulation of a pre-formed receptor array
Irieda, H., Homma, M., Homma, M., and Kawagishi, I.
Journal of Biological Chemistry

281, 23880-23886
2006



The remarkably wide dynamic range of the chemotactic pathway of Escherichia coli, a model signal transduction system, is achieved by methylation/amidation of the transmembrane chemoreceptors, which regulate the histidine kinase CheA in response to extracellular stimuli. The chemoreceptors cluster at a cell pole together with CheA and the adaptor CheW. Several lines of evidence have led to models that assume high cooperativity and sensitivity via collaboration of receptor dimers within a cluster. Here, using in vivo disulfide crosslinking assays, we demonstrate a well-defined arrangement of the aspartate chemoreceptor (Tar). The differential effects of amidation on crosslinking at different positions indicate that amidation alters the relative orientation of Tar dimers to each other (presumably inducing rotational displacements) without much affecting the conformation of the periplasmic domains. Interestingly, the effect of aspartate on crosslinking at any position tested was roughly opposite to that of receptor amidation. Furthermore, amidation attenuated the effects of aspartate by several orders of magnitude. These results suggest that receptor covalent modification controls signal gain by altering the arrangement or packing of receptor dimers in a pre-formed cluster.
25 Research paper (scientific journal)
Joint
The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation
Shih, Y.-L., Kawagishi, I., and Rothfield, L.
Molecular Microbiology

60, 917-928
2005




26 Research paper (scientific journal)
Joint
Only one of the five CheY homologs of Vibrio cholerae directly switches flagellar rotation
Hyakutake, A., Homma, M., Austin, M. J., Boin, M. A., Häse, C. C., and Kawagishi, I.
Journal of Bacteriology

188, 8403-8410
2005




27 Research paper (scientific journal)
Joint
Attractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole
Homma, M., Shiomi, D., Homma, M., and Kawagishi, I.
Proceedings of National Academy of Science, U.S.A.

101, 3462-3467
2004




28 Research paper (scientific journal)
Joint
Simultaneous measurement of sensor-protein dynamics and motility of a single cell by on-chip microcultivation system
Inoue, I., Shiomi, D., Kawagishi, I., and Yasuda K.
Nanobiotechnology

2, 4-8
2004




29 Research paper (scientific journal)
Joint
Stabilization of polar localization of a chemoreceptor via its covalent modifications and its communication with a different chemoreceptor
Shiomi, D., Banno, S., Homma, M., and Kawagishi, I.
Journal of Bacteriology

187, 7647-7654
2004




30 Research paper (scientific journal)
Joint
Targeting of the chemotaxis methylesterase/deamidase CheB to the polar receptor-kinase cluster in an Escherichia coli cell
Banno, S., Shiomi, D., Homma, M., and Kawagishi, I.
Molecular Microbiology

53, 1051-1063
2004




31 Research paper (scientific journal)
Joint
Ion-coupling determinants of Na+-driven and H+-driven flagellar motors
Asai, Y., Yakushi, T., Kawagishi, I., and Homma, M.
Journal of Molecular Biology

327, 453-463
2003




32 Research paper (scientific journal)
Joint
Sensing of cytoplasmic pH by bacterial chemoreceptors involves the linker region that connects the membrane-spanning and the signal-modulating helices
Umemura, T., Matsumoto, Y., Ohnishi, K., Homma, M., and Kawagishi, I.
Journal of Biological Chemistry

277, 1593-1598
2002




33 Research paper (scientific journal)
Joint
Analyses of the roles of the three cheA homologs in chemotaxis of Vibrio cholerae
Gosink, K. K., Kobayashi, R., Kawagishi, I., and Häse, C. C.
Journal of Bacteriology

184, 1767-1771
2002




34 Research paper (scientific journal)
Joint
Intragenic suppressors of a mutation in the aspartate chemoreceptor gene that abolishes binding of the receptor to methyltransferase
Shiomi, D., Homma, M., and Kawagishi, I.
Microbiology

148, 3265-3275
2002




35 Research paper (scientific journal)
Joint
Dual recognition of the bacterial chemoreceptor by chemotaxis-specific domains of the CheR methyltransferase
Shiomi, D., Zhulin, I. B., Homma, M., and Kawagishi, I.
Journal of Biological Chemistry

277, 42325-42333
2002




36 Research paper (scientific journal)
Joint
Flagellin-containing membrane vesicles excreted from Vibrio alginolyticus mutants lacking a polar-flagellar filament
Nishioka, N., Furuno, M., Kawagishi, I., and Homma, M.
Journal of Biochemistry

123, 1169-1173
2000




37 Research paper (scientific journal)
Joint
Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio
Furuno, M., Sato, K., Kawagishi, I., and Homma, M.
Journal of Biochemistry

127, 29-36
2000




38 Research paper (scientific journal)
Joint
Cysteine-scanning mutagenesis of the periplasmic loop regions of PomA, a putative channel component of the sodium-driven flagellar motor in Vibrio alginolyticus
Kojima, S., Shoji, T., Asai, Y., Kawagishi, I., and Homma, M.
Journal of Bacteriology

182, 1001-1007
2000




39 Research paper (scientific journal)
Joint
Mutational analysis of ligand recognition by Tcp, the citrate chemoreceptor of Salmonella enteric serovar Typhimurium
Iwama, T., Nakao, K., Nakazato, H., Yamagata, S. , Homma, M., and Kawagishi, I.
Journal of Bacteriology

182, 1437-1441
2000




40 Research paper (scientific journal)
Joint
The aspartate chemoreceptor Tar is effectively methylated by binding to the methyltransferase mainly through hydrophobic interaction
Shiomi, D., Okumura, H., Homma, M., and Kawagishi, I.
Molecular Microbiology

36, 132-140
2000




41 Research paper (scientific journal)
Joint
A slow-motility phenotype caused by substitutions at residue Asp31 in the PomA channel component of a sodium driven flagellar motor
Kojima, S., Shoji, T., Asai, Y., Kawagishi, I., and Homma, M.
Journal of Bacteriology

182, 3314-3318
2000




42 Research paper (scientific journal)
Joint
Coupling ion specificity of chimeras between H+- and Na+-driven motor proteins, MotB and PomB, in Vibrio polar flagella
Asai, Y., Kawagishi, I., Sockett, R. E., and Homma, M.
EMBO Journal

19, 3639-3648
2000




43 Research paper (scientific journal)
Joint
Suppression by the DNA fragment of the motX promoter region on long flagellar mutants of Vibrio alginolyticus
Furuno, M., Sato, K., Kawagishi, I., and Homma, M.
Microbiology and Immunology

43, 39-43
1999




44 Research paper (scientific journal)
Joint
Na+-driven flagellar motor resistant to phenamil, an amiloride analog, caused by a mutation of putative channel component
Kojima, S., Asai, Y., Atsumi, T., Kawagishi, I., and Homma, M.
Journal of Molecular Biology

285, 1537-1547
1999




45 Research paper (scientific journal)
Joint
The polar flagellar motor of Vibrio cholerae is driven by an Na+-motive force
Kojima, S., Yamamoto, K., Kawagishi, I., and Homma, M.
Journal of Bacteriology

181, 1927-1930
1999




46 Research paper (scientific journal)
Joint
Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region
Nishiyama, S., Maruyama, I. N., Homma, M., and Kawagishi, I.
Journal of Molecular Biology

286, 1275-1284
1999




47 Research paper (scientific journal)
Joint
Conversion of a bacterial warm sensor to a cold sensor by methylation of a single residue in the presence of an attractant
Nishiyama, S., Umemura, T., Nara, T., Homma, M., and Kawagishi, I.
Molecular Microbiology

32, 357-365
1999




48 Research paper (scientific journal)
Joint
Functional interaction between PomA and PomB, the Na+-driven flagellar motor components of Vibrio alginolitycus
Yorimitsu, T., Sato, K., Asai, Y., Kawagishi, I., and Homma, M.
Journal of Bacteriology

181, 5103-5106
1999




49 Research paper (scientific journal)
Joint
Random mutagenesis of the pomA gene encoding a putative channel component of the Na+-driven polar flagellar motor of Vibrio alginolyticus
Kojima, S., Kuroda, M., Kawagishi, I., and Homma, M.
Microbiology

145, 1759-1767
1999




50 Research paper (scientific journal)
Joint
Hybrid motor with the H+- and Na+-driven components can rotate Vibrio polar flagellar motor by using sodium ions
Asai, Y., Kawagishi, I., Sockett, R. E., and Homma, M.
Journal of Bacteriology

181, 6332-6338
1999




51 Research paper (scientific journal)
Joint
Chemotactic adaptation is altered by changes in the carboxy-terminal sequence conserved among the major methyl-accepting chemoreceptors
Okumura, H., Nishiyama, S., Sasaki, A., Homma, M., and Kawagishi, I.
Journal of Bacteriology

180, 1862-1868
1998




52 Research paper (scientific journal)
Joint
Intersubunit interaction between transmembrane helices of the bacterial aspartate chemoreceptor homodimer
Umemura, T., Tatsuno, I., Shibasaki, M., Homma, M., and Kawagishi, I.
Journal of Biological Chemistry

273, 30110-30115
1998




53 Research paper (scientific journal)
Joint
Vibrio alginolyticus mutants resistant to phenamil, a specific inhibitor of the sodium-driven flagellar motors
Kojima, S., Atsumi, T., Muramoto, K., Kudo, S., Kawagishi, I., and Homma, M.
Journal of Molecular Biology

265, 310-318
1997




54 Research paper (scientific journal)
Joint
Uncoupling of ligand-binding affinity of the bacterial serine chemoreceptor from methylation- and temperature-modulated signaling states
Iwama, T., Homma, M., and Kawagishi, I.
Journal of Biological Chemistry

272, 13810-13815
1997




55 Research paper (scientific journal)
Joint
Characterization of polar-flagellar-length mutants in Vibrio alginolyticus
Furuno, M., Atsumi, T., Yamada, T., Kojima, S., Nishioka, N., Kawagishi, I., and Homma, M.
Microbiology

143, 1615-1621
1997




56 Research paper (scientific journal)
Joint
Putative channel components for the fast rotating sodium-driven flagellar motor of a marine bacterium
Asai, Y., Kojima, S., Kato, H., Nishioka, N., Kawagishi, I., and Homma, M.
Journal of Bacteriology

179, 5104-5110
1997




57 Research paper (scientific journal)
Joint
Thermosensing properties of mutant aspartate chemoreceptors with methyl-accepting sites replaced singly or multiply by alanine
Nishiyama, S., Nara, T., Homma, M., Imae, Y., and Kawagishi, I.
Journal of Bacteriology

179, 6573-6580
1997




58 Research paper (scientific journal)
Joint
Cloning of a Vibrio alginolyticus rpoN gene that is required for polar flagellar formation
Kawagishi, I., Nakada, M., Nishioka, N., and Homma, M.
Journal of Bacteriology

179, 6851-6854
1997




59 Research paper (scientific journal)
Joint
Cloning and characterization of motY, a gene coding for a component of the sodium-driven flagellar motor in Vibrio alginolyticus
Okunishi, I., Kawagishi, I., and Homma, M.
Journal of Bacteriology

178, 2409-2415
1996




60 Research paper (scientific journal)
Joint
The sodium driven polar flagellar motor of marine Vibrio as the mechanosensor that regulates lateral flagellar expression
Kawagishi, I., Imagawa, M., Imae, Y., McCarter, L., and Homma, M.
Molecular Microbiology

20, 693-699
1996




61 Research paper (scientific journal)
Joint
Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium
Williams, A. W., Yamaguchi, S., Togashi, F., Aizawa, S.-I., Kawagishi, I., and Macnab, R. M.
Journal of Bacteriology

178, 2960-2970
1996




62 Research paper (scientific journal)
Joint
Characterization of the flagellar hook-length control protein FliK of Salmonella typhimurium and Escherichia coli
Kawagishi, I., Homma, M., Williams, A. W., and Macnab, R. M.
Journal of Bacteriology

178, 954-2959
1996




63 Research paper (scientific journal)
Joint
Effect of viscosity on swimming by the lateral and polar flagella of Vibrio alginolyticus
Atsumi, T., Maekawa, Y., Yamada, T., Kawagishi, I., Imae, Y., and Homma, M.
Journal of Bacteriology

178, 5024-5026
1996




64 Research paper (scientific journal)
Joint
Rotational fluctuation of the sodium-driven flagellar motor inVibrio alginolyticus induced by binding of inhibitors
Muramoto, K., Magariyama, Y., Homma, M., Kawagishi, I., Sugiyama, S., Imae, Y., and Kudo, S.
Journal of Molecular Biology

259, 687-695
1996




65 Research paper (scientific journal)
Joint
Modulation of the thermosensing profile of the Escherichia coli aspartate receptor Tar by covalent modification of its methyl-accepting sites
Nara, T., Kawagishi, I., Nishiyama, S., Homma, M., and Imae, Y.
Journal of Biological Chemistry

271, 17932-17936
1996




66 Research paper (scientific journal)
Joint
Chemotactic responses to an attractant and a repellent by the polar and lateral flagella of Vibrio alginolyticus
Homma, M., Oota, H., Kojima, S., Kawagishi, I., and Imae, Y.
Microbiology

142, 2777-2783
1996




67 Research paper (scientific journal)
Joint
Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer
Tatsuno, I., Homma, M., Oosawa, K., and Kawagishi, I.
Science

274, 423-425
1996




68 Research paper (scientific journal)
Joint
High-speed rotation and speed stability of the sodium-driven flagellar motor in Vibrio alginolyticus
Muramoto, K., Kawagishi, I., Kudo, S., Magariyama, Y., Imae, Y., and Homma, M.
Journal of Molecular Biology

251, 50-58
1995




69 Research paper (scientific journal)
Joint
In vivo sulfhydryl modification of the ligand-binding site of Tsr, the Escherichia coli serine chemoreceptor
Atsumi, T., Maekawa, Y., Yamada, T., Kawagishi, I., Imae, Y., and Homma, M.
Journal of Bacteriology

177, 2218-2221
1995




70 Research paper (scientific journal)
Joint
Isolation of the polar and lateral flagellum-defective mutants in Vibrio alginolyticus and identification of their flagellar driving energy sources
Kawagishi, I., Maekawa, Y., Atsumi, T., Homma, M., and Imae, Y.
Journal of Bacteriology

177, 5158-5160
1995




71 Research paper (scientific journal)
Joint
Simultaneous mesurement of bacterial flagellar rotation rate and swimming speed
Magariyama, Y., Sugiyama, S., Muramoto, K., Kawagishi, I., Imae, Y., and Kudo, S.
Biophysical Journal

69, 2154-2162
1995




72 Research paper (scientific journal)
Joint
Removal of the periplasmic DNase before electroporation enhances efficiency of transformation in the marine bacterium Vibrio alginolyticus
Kawagishi, I., Okunishi, I., Homma, M., and Imae, Y.
Microbiology

140, 2355-2361
1994




73 Research paper (scientific journal)
Joint
Very fast flagellar rotation
Magariyama, Y., Sugiyama, S., Muramoto, K., Maekawa, Y., Kawagishi, I., Imae, Y., and Kudo, S.
Nature

371, 752
1994




74 Research paper (scientific journal)
Joint
Transmembrane signalling by the chimeric chemosensory receptors of Escherichia coli Tsr and Tar with heterologous membrane-spanning regions
Tatsuno, I., Lee, L., Kawagishi, I., Homma, M., and Imae, Y.
Molecular Microbiology

14, 755-762
1994




75 Research paper (scientific journal)
Joint
Organization of the Escherichia coli and Salmonella typhimurium chromosomes between flagellar regions IIIa and IIIb, including a large non-coding regionnce proteins of mammalian and plant pathogens
Raha, M., Kihara, M., Kawagishi, I., and Macnab, R. M.
Journal of General Microbiology

139, 1401-1407
1993




76 Research paper (scientific journal)
Joint
Genetic and biochemical analysis of Salmonella typhimurium FliI, a flagellar protein related to the catalytic subunit of the FoF1 ATPase and to virulence proteins of mammalian and plant pathogens
Dreyfus, G., Williams, A., Kawagishi, I., and Macnab, R. M.
Journal of Bacteriology

175, 3131-3138
1993




77 Research paper (scientific journal)
Joint
Characterization of the fliE genes of the Escherichia coli and Salmonella typhimurium and identification of the FliE protein as a component of the flagellar hook-basal body complex
Müller, V., Jones, C. J., Kawagishi, I., Aizawa, S.-I., and Macnab, R. M.
Journal of Bacteriology

174, 2298-2304
1992




78 Research paper (scientific journal)
Joint
Escherichia coli produces a cytoplasmic α-amylase, AmyA
Raha, M., Kawagishi, I., Müller, V., Irikura, V., and Macnab, R. M.
Journal of Bacteriology

174, 6644-6652
1992




79 Research paper (scientific journal)
Joint
Subdivision of flagellar region III of the Escherichia coli and Salmonella typhimurium chromosomes and identification of two additional flagellar genes
Kawagishi, I., Müller, V., Williams, A. W., Irikura, V., and Macnab, R. M.
Journal of General Microbiology

138, 1051-1065
1992




80 Research paper (scientific journal)
Joint
Export of an N-terminal fragment of Escherichia coli flagellin by a flagellum-specific pathway
Kuwajima, G., Kawagishi, I., Homma, M., Asaka, J.-I., Kondo, E., and Macnab, R. M.
Proceedings of National Academy of Science, U.S.A.

86, 4953-4957
1989