研究者詳細 - 森本　雄祐

論文 - 森本　雄祐

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Short peptides from Late Embryogenesis Abundant (LEA) proteins tune liquid–liquid phase separation and prevent aggregation 査読有り国際誌

Wu Y., Morimoto Y.V., Ikeno S.

Biochemical and Biophysical Research Communications 776 2025年08月

記述言語：英語掲載種別：研究論文（学術雑誌）

Short peptides derived from Late Embryogenesis Abundant (LEA) proteins are critically important because they appear to exert their protective functions through liquid–liquid phase separation (LLPS) in vivo. Excitingly, confocal fluorescence microscopy revealed that green fluorescent protein (GFP) exhibited a heterogeneous intracellular distribution in Escherichia coli cells co-expressing LEA peptides. Guided by this observation, we conducted in vitro LLPS assays and found that the LEA-II and LEA-K peptides attenuated segregative LLPS while enhancing solution stability in the associative LLPS mode. These data support our hypothesis that LEA peptides function as molecular shields that suppress protein aggregation, thereby improving heterologous protein expression.

DOI： 10.1016/j.bbrc.2025.152224

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Cell-to-cell signaling in cell populations with large cell size variability 査読有り国際誌

Yukihisa Hayashida, Chikoo Oosawa, Takuo Yasunaga, Yusuke V. Morimoto

Biophysical Journal 124 ( 6 ) 954 - 962 2025年03月

担当区分：最終著者,　責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

Sizes of multiple cells vary when they communicate with each other. Differences in cell size result in variations in the cell surface area and volume, as well as the number of enzymes and receptors involved in signal transduction. Although heterogeneity in cell size may inhibit uniformity in signaling, cell-to-cell signaling is still possible. The outcome when cell size changes to an extreme degree remains unclear. Hence, we inhibited cell division in Dictyostelium cells, a model organism for signal transduction, to gain insights into the consequences of extreme cell size variations. Measurements of cell signals in this population using fluorescence microscopy indicated that the giant cells can communicate with normal-sized cells by suppressing the signal level. Simulations of signal transduction based on the FitzHugh-Nagumo model also suggested similar results. Our findings suggest that signaling mechanism homogenizes cell-to-cell signaling in response to cell size.

DOI： 10.1016/j.bpj.2024.07.017

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Wireframe DNA Origami Capable of Vertex-protruding Transformation 査読有り国際誌

Ochi Y., Kato W., Tsutsui Y., Gomibuchi Y., Tominaga D., Sakai K., Araki T., Yoshitake S., Yasunaga T., Morimoto Y.V., Maeda K., Taira J., Sato Y.

ChemBioChem 2025年02月

記述言語：英語掲載種別：研究論文（学術雑誌）

Regulating dynamic behavior of the designed molecular structures provides a foundation for the construction of functional molecular devices. DNA nanotechnology allows conformational changes in two-dimensional and three-dimensional DNA origami nanostructures by introducing flexibility between the faces of the structures. However, dynamic transformations in wireframe DNA origami, composed solely of vertices and edges, remain challenging due to vertex-specific flexibility. We report a wireframe DNA origami capable of vertex-protruding transformation between the open- and closed-form with eight protruding vertices. This reversible transformation is driven by DNA hybridization and a toehold-mediated strand displacement reaction. Spacer strands between vertices and edges were designed to introduce flexibility. Coarse-grained molecular dynamics simulations demonstrated that a longer spacer increases conformational flexibility and can achieve the narrow angles required for the vertex-protruding transformation. The experimental results showed the successful assembly of the open-form structure under optimized salt conditions, as visualized through transmission electron microscopy images. Furthermore, the transformation between the open- and closed-form structures was demonstrated by the sequential addition of signal strands. This vertex-protruding transformation mechanism will expand the design approach of dynamic DNA nanostructures and help develop functional molecular devices for artificial molecular systems.

DOI： 10.1002/cbic.202401071

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Ion Signaling in Cell Motility and Development in Dictyostelium discoideum 査読有り国際誌

Morimoto Y.V.

Biomolecules 14 ( 7 ) 2024年07月

担当区分：筆頭著者,　最終著者,　責任著者記述言語：英語掲載種別：記事・総説・解説・論説等（学術雑誌）

Cell-to-cell communication is fundamental to the organization and functionality of multicellular organisms. Intercellular signals orchestrate a variety of cellular responses, including gene expression and protein function changes, and contribute to the integrated functions of individual tissues. Dictyostelium discoideum is a model organism for cell-to-cell interactions mediated by chemical signals and multicellular formation mechanisms. Upon starvation, D. discoideum cells exhibit coordinated cell aggregation via cyclic adenosine 3′,5′-monophosphate (cAMP) gradients and chemotaxis, which facilitates the unicellular-to-multicellular transition. During this process, the calcium signaling synchronizes with the cAMP signaling. The resulting multicellular body exhibits organized collective migration and ultimately forms a fruiting body. Various signaling molecules, such as ion signals, regulate the spatiotemporal differentiation patterns within multicellular bodies. Understanding cell-to-cell and ion signaling in Dictyostelium provides insight into general multicellular formation and differentiation processes. Exploring cell-to-cell and ion signaling enhances our understanding of the fundamental biological processes related to cell communication, coordination, and differentiation, with wide-ranging implications for developmental biology, evolutionary biology, biomedical research, and synthetic biology. In this review, I discuss the role of ion signaling in cell motility and development in D. discoideum.

DOI： 10.3390/biom14070830

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Frontiers of microbial movement research 査読有り国際誌

Minamino T., Nakane D., Nakamura S., Kiyama H., Morimoto Y.V., Miyata M.

Biophysics and physicobiology 20 ( 3 ) 2023年08月

Visualization of c-di-GMP in multicellular Dictyostelium stages 査読有り国際誌

Ide H., Hayashida Y., Morimoto Y.V.

Frontiers in Cell and Developmental Biology 11 2023年07月

担当区分：最終著者,　責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

The bacterial signaling molecule cyclic diguanosine monophosphate (c-di-GMP) is only synthesized and utilized by the cellular slime mold Dictyostelium discoideum among eukaryotes. Dictyostelium cells undergo a transition from a unicellular to a multicellular state, ultimately forming a stalk and spores. While Dictyostelium is known to employ c-di-GMP to induce differentiation into stalk cells, there have been no reports of direct observation of c-di-GMP using fluorescent probes. In this study, we used a fluorescent probe used in bacteria to visualize its localization within Dictyostelium multicellular bodies. Cytosolic c-di-GMP concentrations were significantly higher at the tip of the multicellular body during stalk formation.

DOI： 10.3389/fcell.2023.1237778

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細胞性粘菌におけるシグナル伝達の高感度な可視化招待有り

森本雄祐, 橋村秀典

月刊細胞 55 ( 5 ) 37 - 40 2023年03月

Measurements of the Ion Channel Activity of the Transmembrane Stator Complex in the Bacterial Flagellar Motor 招待有り査読有り国際誌

Morimoto Y.V., Minamino T.

Methods in molecular biology (Clifton, N.J.) 2646 83 - 94 2023年01月

担当区分：筆頭著者,　責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

The bacterial flagellum is driven by a rotational motor located at the base of the flagellum. The stator unit complex conducts cations such as protons (H+) and sodium ions (Na+) along the electrochemical potential across the cytoplasmic membrane and interacts with the rotor to generate the rotational force. Escherichia coli and Salmonella have the H+-type stator complex, which serves as a transmembrane H+ channel that couples H+ flow through an ion channel to torque generation whereas Vibrio and some Bacillus species have the Na+-type stator complex. In this chapter, we describe how to measure the ion conductivity of the transmembrane stator complex over-expressed in E. coli cells using fluorescent indicators. Intensity measurements of fluorescent indicators using either a fluorescence spectrophotometer or microscope allow quantitative detection of changes in the intracellular ion concentrations due to the ion channel activity of the transmembrane protein complex.

DOI： 10.1007/978-1-0716-3060-0_8

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Activation mechanism of the bacterial flagellar dual-fuel protein export engine 招待有り査読有り国際誌

Minamino T., Kinoshita M., Morimoto Y.V., Namba K.

Biophysics and physicobiology 19 2022年12月

記述言語：英語掲載種別：記事・総説・解説・論説等（学術雑誌）

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 cytoplasmic ATPase ring complex. The transmembrane export gate complex is fueled by proton motive force across the cytoplasmic membrane and is divided into four distinct functional parts: a dual-fuel export engine; a polypeptide channel; a membrane voltage sensor; and a docking platform. ATP hydrolysis by the cytoplasmic ATPase complex converts the export gate complex into a highly efficient proton (H+)/ protein antiporter that couples inward-directed H+ flow with outward-directed protein export. When the ATPase ring complex does not work well in a given environment, the export gate complex will remain inactive. However, when the electric potential difference, which is defined as membrane voltage, rises above a certain threshold value, the export gate complex becomes an active H+ /protein antiporter to a considerable degree, suggesting that the export gate complex has a voltage-gated activation mechanism. Furthermore, the export gate complex also has a sodium ion (Na+) channel to couple Na+ influx with flagellar protein export. In this article, we review our current understanding of the activation mechanism of the dual-fuel protein export engine of the fT3SS. This review article is an extended version of a Japanese article, Membrane voltage-dependent activation of the transmembrane export gate complex in the bacterial flagellar type III secretion system, published in SEIBUTSU BUTSURI Vol. 62, p165–169 (2022).

DOI： 10.2142/biophysico.bppb-v19.0046

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Calcium responses to external mechanical stimuli in the multicellular stage of Dictyostelium discoideum 査読有り国際誌

Hashimura H., Morimoto Y.V., Hirayama Y., Ueda M.

Scientific Reports 12 ( 1 ) 2022年07月

担当区分：筆頭著者,　責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

Calcium acts as a second messenger to regulate many cellular functions, including cell motility. In Dictyostelium discoideum, the cytosolic calcium level oscillates synchronously, and calcium waves propagate through the cell population during the early stages of development, including aggregation. In the unicellular phase, the calcium response through Piezo channels also functions in mechanosensing. However, calcium dynamics during multicellular morphogenesis are still unclear. Here, live imaging of cytosolic calcium revealed that calcium wave propagation, depending on cAMP relay, disappeared at the onset of multicellular body (slug) formation. Later, other forms of occasional calcium bursts and their propagation were observed in both anterior and posterior regions of migrating slugs. This calcium signaling also occurred in response to mechanical stimuli. Two pathways—calcium release from the endoplasmic reticulum via IP3 receptor and calcium influx from outside the cell—were involved in calcium signals induced by mechanical stimuli. These data suggest that calcium signaling is involved in mechanosensing in both the unicellular and multicellular phases of Dictyostelium development using different molecular mechanisms.

DOI： 10.1038/s41598-022-16774-3

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細菌べん毛輸送装置の膜電位に依存した活性化機構査読有り

南野徹, 木下実紀, 森本雄祐, 難波啓一

生物物理 62 ( 3 ) 165 - 169 2022年05月

Light dependent synthesis of a nucleotide second messenger controls the motility of a spirochete bacterium 査読有り国際誌

Xu J., Koizumi N., Morimoto Y.V., Ozuru R., Masuzawa T., Nakamura S.

Scientific Reports 12 ( 1 ) 2022年04月

担当区分：筆頭著者記述言語：英語掲載種別：研究論文（学術雑誌）

Nucleotide second messengers are universally crucial factors for the signal transduction of various organisms. In prokaryotes, cyclic nucleotide messengers are involved in the bacterial life cycle and in functions such as virulence and biofilm formation, mainly via gene regulation. Here, we show that the swimming motility of the soil bacterium Leptospira kobayashii is rapidly modulated by light stimulation. Analysis of a loss-of-photoresponsivity mutant obtained by transposon random mutagenesis identified the novel sensory gene, and its expression in Escherichia coli through codon optimization elucidated the light-dependent synthesis of cyclic adenosine monophosphate (cAMP). GFP labeling showed the localization of the photoresponsive enzyme at the cell poles where flagellar motors reside. These findings suggest a new role for cAMP in rapidly controlling the flagella-dependent motility of Leptospira and highlight the global distribution of the newly discovered photoactivated cyclase among diverse microbial species.

DOI： 10.1038/s41598-022-10556-7

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Multiple Roles of Flagellar Export Chaperones for Efficient and Robust Flagellar Filament Formation in Salmonella 査読有り国際誌

Minamino T., Morimoto Y.V., Kinoshita M., Namba K.

Frontiers in Microbiology 12 2021年10月

記述言語：英語掲載種別：研究論文（学術雑誌）

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 transmembrane export gate protein, FlhA, to facilitate their subsequent unfolding and export by the flagellar type III secretion system (fT3SS). Dynamic interactions of the chaperones with FlhA are thought to determine the substrate export order. To clarify the role of flagellar chaperones in filament assembly, we constructed cells lacking FlgN, FliS, and/or FliT. Removal of either FlgN, FliS, or FliT resulted in leakage of a large amount of unassembled FliC monomers into the culture media, indicating that these chaperones contribute to robust and efficient filament formation. The ∆flgN ∆fliS ∆fliT (∆NST) cells produced short filaments similarly to the ∆fliS mutant. Suppressor mutations of the ∆NST cells, which lengthened the filament, were all found in FliC and destabilized the folded structure of FliC monomer. Deletion of FliS inhibited FliC export and filament elongation only after FliC synthesis was complete. We propose that FliS is not involved in the transport of FliC upon onset of filament formation, but FliS-assisted unfolding of FliC by the fT3SS becomes essential for its rapid and efficient export to form a long filament when FliC becomes fully expressed in the cytoplasm.

DOI： 10.3389/fmicb.2021.756044

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Membrane voltage-dependent activation mechanism of the bacterial flagellar protein export apparatus 査読有り国際誌

Minamino T., Morimoto Y.V., Kinoshita M., Namba K.

Proceedings of the National Academy of Sciences of the United States of America 118 ( 22 ) 2021年06月

記述言語：英語掲載種別：研究論文（学術雑誌）

The proton motive force (PMF) consists of the electric potential difference (Δψ), which is measured as membrane voltage, and the proton concentration difference (ΔpH) across the cytoplasmic membrane. The flagellar protein export machinery is composed of a PMF-driven transmembrane export gate complex and a cytoplasmic ATPase ring complex consisting of FliH, FliI, and FliJ. ATP hydrolysis by the FliI ATPase activates the export gate complex to become an active protein transporter utilizing Δψ to drive proton-coupled protein export. An interaction between FliJ and a transmembrane ion channel protein, FlhA, is a critical step for Δψ-driven protein export. To clarify how Δψ is utilized for flagellar protein export, we analyzed the export properties of the export gate complex in the absence of FliH and FliI. The protein transport activity of the export gate complex was very low at external pH 7.0 but increased significantly with an increase in Δψ by an upward shift of external pH from 7.0 to 8.5. This observation suggests that the export gate complex is equipped with a voltage-gated mechanism. An increase in the cytoplasmic level of FliJ and a gain-of-function mutation in FlhA significantly reduced the Δψ dependency of flagellar protein export by the export gate complex. However, deletion of FliJ decreased Δψ-dependent protein export significantly. We propose that Δψ is required for efficient interaction between FliJ and FlhA to open the FlhA ion channel to conduct protons to drive flagellar protein export in a Δψ-dependent manner.

DOI： 10.1073/pnas.2026587118

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The FlgN chaperone activates the Na+-driven engine of the Salmonella flagellar protein export apparatus 査読有り国際誌

Minamino T., Kinoshita M., Morimoto Y.V., Namba K.

Communications Biology 4 ( 1 ) 335 2021年03月

記述言語：英語掲載種別：研究論文（学術雑誌）

© 2021, The Author(s). The bacterial flagellar protein export machinery consists of a transmembrane export gate complex and a cytoplasmic ATPase complex. The gate complex has two intrinsic and distinct H+-driven and Na+-driven engines to drive the export of flagellar structural proteins. Salmonella wild-type cells preferentially use the H+-driven engine under a variety of environmental conditions. To address how the Na+-driven engine is activated, we analyzed the fliJ(Δ13–24) fliH(Δ96–97) mutant and found that the interaction of the FlgN chaperone with FlhA activates the Na+-driven engine when the ATPase complex becomes non-functional. A similar activation can be observed with either of two single-residue substitutions in FlhA. Thus, it is likely that the FlgN-FlhA interaction generates a conformational change in FlhA that allows it to function as a Na+ channel. We propose that this type of activation would be useful for flagellar construction under conditions in which the proton motive force is severely restricted.

DOI： 10.1038/s42003-021-01865-0

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Architecture and Assembly of the Bacterial Flagellar Motor Complex 招待有り査読有り国際誌

Morimoto Y.V., Minamino T.

Subcellular Biochemistry 96 297 - 321 2021年01月

担当区分：筆頭著者記述言語：英語掲載種別：記事・総説・解説・論説等（学術雑誌）

© 2021, Springer Nature Switzerland AG. One of the central systems responsible for bacterial motility is the flagellum. The bacterial flagellum is a macromolecular protein complex that is more than five times the cell length. Flagella-driven motility is coordinated via a chemosensory signal transduction pathway, and so bacterial cells sense changes in the environment and migrate towards more desirable locations. The flagellum of Salmonella enterica serovar Typhimurium is composed of a bi-directional rotary motor, a universal joint and a helical propeller. The flagellar motor, which structurally resembles an artificial motor, is embedded within the cell envelop and spins at several hundred revolutions per second. In contrast to an artificial motor, the energy utilized for high-speed flagellar motor rotation is the inward-directed proton flow through a transmembrane proton channel of the stator unit of the flagellar motor. The flagellar motor realizes efficient chemotaxis while performing high-speed movement by an ingenious directional switching mechanism of the motor rotation. To build the universal joint and helical propeller structures outside the cell body, the flagellar motor contains its own protein transporter called a type III protein export apparatus. In this chapter we summarize the structure and assembly of the Salmonella flagellar motor complex.

DOI： 10.1007/978-3-030-58971-4_8

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Distinct chemotactic behavior in the original Escherichia coli K-12 depending on forward-and-backward swimming, not on run-tumble movements 査読有り国際誌

Kinosita Y., Ishida T., Yoshida M., Ito R., Morimoto Y.V., Goto K., Berry R.M., Nishizaka T., Sowa Y.

Scientific Reports 10 ( 1 ) 2020年09月

記述言語：英語掲載種別：研究論文（学術雑誌）

© 2020, The Author(s). Most motile bacteria are propelled by rigid, helical, flagellar filaments and display distinct swimming patterns to explore their favorable environments. Escherichia coli cells have a reversible rotary motor at the base of each filament. They exhibit a run-tumble swimming pattern, driven by switching of the rotational direction, which causes polymorphic flagellar transformation. Here we report a novel swimming mode in E. coli ATCC10798, which is one of the original K-12 clones. High-speed tracking of single ATCC10798 cells showed forward and backward swimming with an average turning angle of 150°. The flagellar helicity remained right-handed with a 1.3 μm pitch and 0.14 μm helix radius, which is consistent with the feature of a curly type, regardless of motor switching; the flagella of ATCC10798 did not show polymorphic transformation. The torque and rotational switching of the motor was almost identical to the E. coli W3110 strain, which is a derivative of K-12 and a wild-type for chemotaxis. The single point mutation of N87K in FliC, one of the filament subunits, is critical to the change in flagellar morphology and swimming pattern, and lack of flagellar polymorphism. E. coli cells expressing FliC(N87K) sensed ascending a chemotactic gradient in liquid but did not spread on a semi-solid surface. Based on these results, we concluded that a flagellar polymorphism is essential for spreading in structured environments.

DOI： 10.1038/s41598-020-72429-1

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GFP Fusion to the N-Terminus of MotB Affects the Proton Channel Activity of the Bacterial Flagellar Motor in Salmonella 査読有り国際誌

Morimoto Y.V., Namba K., Minamino T.

Biomolecules 10 ( 9 ) 2020年08月

担当区分：筆頭著者記述言語：英語掲載種別：研究論文（学術雑誌）

The bacterial flagellar motor converts the energy of proton flow through the MotA/MotB complex into mechanical works required for motor rotation. The rotational force is generated by electrostatic interactions between the stator protein MotA and the rotor protein FliG. The Arg-90 and Glu-98 from MotA interact with Asp-289 and Arg-281 of FliG, respectively. An increase in the expression level of the wild-type MotA/MotB complex inhibits motility of the gfp-motBfliG(R281V) mutant but not the fliG(R281V) mutant, suggesting that the MotA/GFP-MotB complex cannot work together with wild-type MotA/MotB in the presence of the fliG(R281V) mutation. However, it remains unknown why. Here, we investigated the effect of the GFP fusion to MotB at its N-terminus on the MotA/MotB function. Over-expression of wild-type MotA/MotB significantly reduced the growth rate of the gfp-motBfliG(R281V) mutant. The over-expression of the MotA/GFP-MotB complex caused an excessive proton leakage through its proton channel, thereby inhibiting cell growth. These results suggest that the GFP tag on the MotB N-terminus affects well-regulated proton translocation through the MotA/MotB proton channel. Therefore, we propose that the N-terminal cytoplasmic tail of MotB couples the gating of the proton channel with the MotA-FliG interaction responsible for torque generation.

DOI： 10.3390/biom10091255

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Direct observation of speed fluctuations of flagellar motor rotation at extremely low load close to zero 査読有り国際誌

Nakamura S., Hanaizumi Y., Morimoto Y., Inoue Y., Erhardt M., Minamino T., Namba K.

Molecular Microbiology 2020年04月

記述言語：英語掲載種別：研究論文（学術雑誌）

© 2019 John Wiley & Sons Ltd The bacterial flagellar motor accommodates ten stator units around the rotor to produce large torque at high load. But when external load is low, some previous studies showed that a single stator unit can spin the rotor at the maximum speed, suggesting that the maximum speed does not depend on the number of active stator units, whereas others reported that the speed is also dependent on the stator number. To clarify these two controversial observations, much more precise measurements of motor rotation would be required at external load as close to zero as possible. Here, we constructed a Salmonella filament-less mutant that produces a rigid, straight, twice longer hook to efficiently label a 60 nm gold particle and analyzed flagellar motor dynamics at low load close to zero. The maximum motor speed was about 400 Hz. Large speed fluctuations and long pausing events were frequently observed, and they were suppressed by either over-expression of the MotAB stator complex or increase in the external load, suggesting that the number of active stator units in the motor largely fluctuates near zero load. We conclude that the lifetime of the active stator unit becomes much shorter when the motor operates near zero load.

DOI： 10.1111/mmi.14440

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Talin B regulates collective cell migration via PI3K signaling in Dictyostelium discoideum mounds 査読有り国際誌

Yamazaki S.i., Hashimura H., Morimoto Y.V., Miyanaga Y., Matsuoka S., Kamimura Y., Ueda M.

Biochemical and Biophysical Research Communications 2020年02月

記述言語：英語掲載種別：研究論文（学術雑誌）

© 2020 The Author(s) Collective cell migration is a key process during the development of multicellular organisms, in which the migrations of individual cells are coordinated through chemical guidance and physical contact between cells. Talin has been implicated in mechanical linkage between actin-based motile machinery and adhesion molecules, but how talin contributes to collective cell migration is unclear. Here we show that talin B is involved in chemical coordination between cells for collective cell migration at the multicellular mound stage in the development of Dictyostelium discoideum. From early aggregation to the mound formation, talB-null cells exhibited collective migration normally with cAMP relay. Subsequently, talB-null cells showed developmental arrest at the mound stage, and at the same time, they had impaired collective migration and cAMP relay, while wild-type cells exhibited rotational cell migration continuously in concert with cAMP relay during the mound stage. Genetic suppression of PI3K activity partially restored talB-null phenotypes in collective cell migration and cAMP relay. Overall, our observations suggest that talin B regulates chemical coordination via PI3K-mediated signaling in a stage-specific manner for the multicellular development of Dictyostelium cells.

DOI： 10.1016/j.bbrc.2020.02.060

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