Details of the Researcher

PHOTO

Shinya Tahara
Section
Graduate School of Pharmaceutical Sciences
Job title
Assistant Professor
Degree
e-Rad No.
00783060

Research History 3

  • 2020/09 - Present
    Tohoku University　Graduate School of Pharmaceutical Sciences　Assistant professor

  • 2018/04 - 2020/08
    Osaka University

  • 2016/04 - 2018/03
    理化学研究所　田原分子分光研究室　特別研究員

Education 3

  • 東京工業大学大学院　生体分子機能工学専攻 博士課程

    2013/04 - 2016/03

  • 東京工業大学大学院　生体分子機能工学専攻 修士課程

    2011/04 - 2013/03

  • Tokyo Institute of Technology　School of Bioscience and Biotechnology

    2007/04 - 2011/03

Professional Memberships 5

  • 日本光医学・光生物学会

  • 日本生物物理学会

  • 日本蛋白質科学会

  • 日本薬学会

  • JAPAN SOCIETY FOR MOLECULAR SCIENCE

Research Interests 4

  • 液-液相分離

  • 顕微分光

  • ラマン分光

  • 神経変性疾患

Research Areas 3

  • Natural sciences / Bio-, chemical, and soft-matter physics /

  • Life sciences / Biophysics /

  • Nanotechnology/Materials / Basic physical chemistry /

Awards 4

  1. 奨励賞(生物・化学領域)

    2023/06　日本光医学・光生物学会

  2. 優秀講演賞(学術)

    2019/03　日本化学会

  3. 年次講演会若手講演賞

    2017/05　日本分光学会

  4. 分子科学会優秀講演賞

    2015/09　分子科学会

Papers 22

  1. Liquid–liquid phase separation-assisted Raman microscopy for sensitive and label-free analysis of enzymatic reactions and protein–small molecule interactions Peer-reviewed

    Lisa Kageyama, Shinya Tahara, Reona Tobita, Shinji Kajimoto, Takakazu Nakabayashi

    Analyst　151　807-815　2026/02

    Publisher: Royal Society of Chemistry (RSC)

    DOI： 10.1039/d5an00973a 　

    ISSN： 0003-2654

    eISSN： 1364-5528

    More details Close

    High-concentration PEG-based liquid–liquid phase separation concentrates biomolecules into droplets, enabling highly sensitive, label-free Raman analysis of enzymatic reactions and protein–small-molecule interactions in dilute, small-volume samples.

  2. Molecular Mechanism of Metal-Ion-Induced Protofibril Formation of Ataxin-3 Peer-reviewed

    Ippei Suzuki, Shinya Tahara, Nozomi Goso, Takahiro Morito, Dai Kato, Yusuke Hatakawa, Seon Hwa Lee, Tomoyuki Oe, Kunisato Kuroi, Takakazu Nakabayashi

    Bulletin of the Chemical Society of Japan　2026/01/22

    Publisher: Oxford University Press (OUP)

    DOI： 10.1093/bulcsj/uoag009 　

    ISSN： 0009-2673

    eISSN： 1348-0634

    More details Close

    Abstract Ataxin-3, the causative protein of Machado-Joseph disease, comprises an enzymatic domain, Josephin domain (JD), and a polyglutamine repeat (polyQ). The polyQ expansion promotes the fibrillogenesis of ataxin-3, which is responsible for the disease onset. The fibrillogenesis proceeds through two distinct steps: protofibril formation, in which JD undergoes self-assembly, and subsequent fibrillation. Both polyQ elongation and metal ions accelerate fibrillation; however, the effects of these factors on each stage remain unclear. This study comprehensively analyzed the effects of metal ions on ataxin-3 protofibril formation using spectroscopic analyses. The protofibril formation of JD and a 28-residue polyQ tract (Q28) did not complete within 14 days under metal-free conditions. In contrast, the introduction of Cu²⁺ or Zn²⁺ markedly accelerated the process: JD denatured within one day, and protofibrils formed within four days. The acceleration was similar between JD and Q28, indicating that metal binding primarily affects JD. SH assays and mass spectrometry showed that Cu²⁺ binds to thiols and induces intra- and intermolecular disulfide bonds, whereas Zn²⁺ binds to thiols but does not promote disulfide formation. These observations suggest that Cu²⁺ and Zn²⁺ enhance the protofibril formation through interactions with specific JD sites, but the underlying mechanisms differ between the two metal ions.

  3. RNA-Mediated Inhibition Mechanism of Liquid–Liquid Phase Separation and Subsequent Aggregation Revealed by Raman Microscopy Peer-reviewed

    Taisei Ogura, Uchu Matsuura, Masato Machida, Kaichi Nagai, Shinji Kajimoto, Shinya Tahara, Takakazu Nakabayashi

    JACS Au　5　(11)　5749-5757　2025/11/03

    Publisher: American Chemical Society (ACS)

    DOI： 10.1021/jacsau.5c01234 　

    ISSN： 2691-3704

    eISSN： 2691-3704

  4. Liquid–Liquid Phase Separation from the Viewpoint of Molecular Crowding Environment: A Raman Imaging Study Peer-reviewed

    Takakazu Nakabayashi, Shinya Tahara, Shinji Kajimoto

    The Journal of Physical Chemistry B　129　(32)　8087-8098　2025/08/04

    Publisher: American Chemical Society (ACS)

    DOI： 10.1021/acs.jpcb.5c02288 　

    ISSN： 1520-6106

    eISSN： 1520-5207

  5. 液-液相分離したタンパク質のダイナミクスを可視化する顕微分光学的手法 Peer-reviewed

    田原進也

    Photomedicine and Photobiology　46　1-6　2025/07

  6. Ultrafast Protein Dynamics Prior to Retinal Photoisomerization in Microbial Rhodopsins Peer-reviewed

    Shinya Tahara, Rika Kurihara, Keiichi Kojima, Hikaru Kuramochi, Satoshi Takeuchi, Yuki Sudo, Tahei Tahara

    The Journal of Physical Chemistry Letters　16　(23)　5732-5738　2025/06/02

    Publisher: American Chemical Society (ACS)

    DOI： 10.1021/acs.jpclett.5c00623 　

    ISSN： 1948-7185

    eISSN： 1948-7185

  7. Raman quantitative analysis of methionine oxidation and its promotion effect on dissolution of phase-separated liquid droplets of Pbp1 Peer-reviewed

    Lisa Kageyama, Shinya Tahara, Kohei Yokosawa, Mana Kamijo, Shinji Kajimoto, Takakazu Nakabayashi

    Chemical Physics Letters　856　141671-141671　2024/12

    Publisher: Elsevier BV

    DOI： 10.1016/j.cplett.2024.141671 　

    ISSN： 0009-2614

  8. Highly sensitive Raman measurements of protein aqueous solutions using liquid–liquid phase separation Peer-reviewed

    Reona Tobita, Lisa Kageyama, Ayaka Saito, Shinya Tahara, Shinji Kajimoto, Takakazu Nakabayashi

    Chemical Communications　60　8732-8735　2024

    Publisher: Royal Society of Chemistry (RSC)

    DOI： 10.1039/d4cc03035d 　

    ISSN： 1359-7345

    eISSN： 1364-548X

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    A highly sensitive method is proposed for obtaining the Raman spectra of low-concentration proteins and nucleic acids in an aqueous solution using liquid–liquid phase separation.

  9. Visualization of the sequence of changes in the full wavenumber range by two-dimensional correlation spectroscopy Peer-reviewed

    Kazunori Ban, Daisuke Miyata, Yoshiteru Matsumoto, Shinya Tahara, Hiroaki Takahashi, Shin-ichi Morita, Takakazu Nakabayashi

    Chemical Physics Letters　833　(16)　140930　2023/11

    Publisher: Elsevier BV

    DOI： 10.1016/j.cplett.2023.140930 　

    ISSN： 0009-2614

  10. Label-free autofluorescence lifetime reveals the structural dynamics of ataxin-3 inside droplets formed via liquid–liquid phase separation Peer-reviewed

    Uchu Matsuura, Shinya Tahara, Shinji Kajimoto, Takakazu Nakabayashi

    Scientific Reports　13　(1)　6389　2023/04/19

    Publisher: Springer Science and Business Media LLC

    DOI： 10.1038/s41598-023-33268-y 　

    eISSN： 2045-2322

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    Abstract Liquid–liquid phase separation is a phenomenon that features the formation of liquid droplets containing concentrated solutes. The droplets of neurodegeneration-associated proteins are prone to generate aggregates and cause diseases. To uncover the aggregation process from the droplets, it is necessary to analyze the protein structure with keeping the droplet state in a label-free manner, but there was no suitable method. In this study, we observed the structural changes of ataxin-3, a protein associated with Machado–Joseph disease, inside the droplets, using autofluorescence lifetime microscopy. Each droplet showed autofluorescence due to tryptophan (Trp) residues, and its lifetime increased with time, reflecting structural changes toward aggregation. We used Trp mutants to reveal the structural changes around each Trp and showed that the structural change consists of several steps on different timescales. We demonstrated that the present method visualizes the protein dynamics inside a droplet in a label-free manner. Further investigations revealed that the aggregate structure formed in the droplets differs from that formed in dispersed solutions and that a polyglutamine repeat extension in ataxin-3 hardly modulates the aggregation dynamics in the droplets. These findings highlight that the droplet environment facilitates unique protein dynamics different from those in solutions.

  11. General Design Strategy to Precisely Control the Emission of Fluorophores via a Twisted Intramolecular Charge Transfer (TICT) Process International-journal Peer-reviewed

    Kenjiro Hanaoka, Shimpei Iwaki, Kiyoshi Yagi, Takuya Myochin, Takayuki Ikeno, Hisashi Ohno, Eita Sasaki, Toru Komatsu, Tasuku Ueno, Motokazu Uchigashima, Takayasu Mikuni, Kazuki Tainaka, Shinya Tahara, Satoshi Takeuchi, Tahei Tahara, Masanobu Uchiyama, Tetsuo Nagano, Yasuteru Urano

    Journal of the American Chemical Society　144　(43)　19778-19790　2022/11/02

    Publisher: American Chemical Society (ACS)

    DOI： 10.1021/jacs.2c06397 　

    ISSN： 0002-7863

    eISSN： 1520-5126

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    Fluorogenic probes for bioimaging have become essential tools for life science and medicine, and the key to their development is a precise understanding of the mechanisms available for fluorescence off/on control, such as photoinduced electron transfer (PeT) and Förster resonance energy transfer (FRET). Here we establish a new molecular design strategy to rationally develop activatable fluorescent probes, which exhibit a fluorescence off/on change in response to target biomolecules, by controlling the twisted intramolecular charge transfer (TICT) process. This approach was developed on the basis of a thorough investigation of the fluorescence quenching mechanism of N-phenyl rhodamine dyes (commercially available as the QSY series) by means of time-dependent density functional theory (TD-DFT) calculations and photophysical evaluation of their derivatives. To illustrate and validate this TICT-based design strategy, we employed it to develop practical fluorogenic probes for HaloTag and SNAP-tag. We further show that the TICT-controlled fluorescence off/on mechanism is generalizable by synthesizing a Si-rhodamine-based fluorogenic probe for HaloTag, thus providing a palette of chemical dyes that spans the visible and near-infrared range.

  12. SOD1 gains pro-oxidant activity upon aberrant oligomerization: change in enzymatic activity by intramolecular disulfide bond cleavage Peer-reviewed

    Kosuke Yamazaki, Shinya Tahara, Takumi Ohyama, Kunisato Kuroi, Takakazu Nakabayashi

    Scientific Reports　12　(1)　11750　2022/07

    Publisher: Springer Science and Business Media LLC

    DOI： 10.1038/s41598-022-15701-w 　

    eISSN： 2045-2322

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    Abstract Copper-zinc superoxide dismutase (SOD1) has been proposed as one of the causative proteins of amyotrophic lateral sclerosis (ALS). The accumulation of non-native conformers, oligomers, and aggregates of SOD1 in motor neurons is considered responsible for this disease. However, it remains unclear which specific feature of these species induces the onset of ALS. In this study, we showed that disulfide-linked oligomers of denatured SOD1 exhibit pro-oxidant activity. Substituting all the cysteine residues in the free thiol state with serine resulted in the loss of both the propensity to oligomerize and the increase in pro-oxidant activity after denaturation. In contrast, these cysteine mutants oligomerized and acquired the pro-oxidant activity after denaturation in the presence of a reductant that cleaves the intramolecular disulfide bond. These results indicate that one of the toxicities of SOD1 oligomers is the pro-oxidant activity induced by scrambling of the disulfide bonds. Small oligomers such as dimers and trimers exhibit stronger pro-oxidant activity than large oligomers and aggregates, consistent with the trend of the cytotoxicity of oligomers and aggregates reported in previous studies. We propose that the cleavage of the intramolecular disulfide bond accompanied by the oligomerization reduces the substrate specificity of SOD1, leading to the non-native enzymatic activity.

  13. Frontispiz: Mode‐Specific Vibrational Analysis of Exciton Delocalization and Structural Dynamics in Conjugated Oligomers Peer-reviewed

    Woojae Kim, Shinya Tahara, Hikaru Kuramochi, Satoshi Takeuchi, Taeyeon Kim, Tahei Tahara, Dongho Kim

    Angewandte Chemie　133　(31)　17136-17145　2021/07/26

    Publisher: Wiley

    DOI： 10.1002/ange.202183162 　

  14. Mode‐Specific Vibrational Analysis of Exciton Delocalization and Structural Dynamics in Conjugated Oligomers Peer-reviewed

    Woojae Kim, Shinya Tahara, Hikaru Kuramochi, Satoshi Takeuchi, Taeyeon Kim, Tahei Tahara, Dongho Kim

    Angewandte Chemie International Edition　60　(31)　16999-17008　2021/03/17

    Publisher: Wiley

    DOI： 10.1002/anie.202102168 　

    ISSN： 1433-7851

    eISSN： 1521-3773

  15. Nonbonded Atomic Contacts Drive Ultrafast Helix Motions in Myoglobin Peer-reviewed

    Shinya Tahara, Misao Mizuno, Yasuhisa Mizutani

    The Journal of Physical Chemistry B　124　(26)　5407-5414　2020/07/02

    Publisher: American Chemical Society (ACS)

    DOI： 10.1021/acs.jpcb.0c04772 　

    ISSN： 1520-6106

    eISSN： 1520-5207

  16. Protein Dynamics Preceding Photoisomerization of the Retinal Chromophore in Bacteriorhodopsin Revealed by Deep-UV Femtosecond Stimulated Raman Spectroscopy Peer-reviewed

    Shinya Tahara, Hikaru Kuramochi, Satoshi Takeuchi, Tahei Tahara

    The Journal of Physical Chemistry Letters　10　(18)　5422-5427　2019/09/19

    Publisher: American Chemical Society (ACS)

    DOI： 10.1021/acs.jpclett.9b02283 　

    ISSN： 1948-7185

    eISSN： 1948-7185

  17. Ultrafast Dynamics of Heliorhodopsins. International-journal Peer-reviewed

    Shinya Tahara, Manish Singh, Hikaru Kuramochi, Wataru Shihoya, Keiichi Inoue, Osamu Nureki, Oded Béjà, Yasuhisa Mizutani, Hideki Kandori, Tahei Tahara

    The journal of physical chemistry. B　123　(11)　2507-2512　2019/03/21

    DOI： 10.1021/acs.jpcb.9b00887 　

    ISSN： 1520-6106

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    Heliorhodopsins (HeR) constitute a new rhodopsin family and show only <15% sequence identities with type-1 and type-2 rhodopsins. The large difference in amino acid sequence between HeRs and other rhodopsins raises a question whether their biological function is triggered by efficient and rapid photoisomerization of the retinal chromophore as in the case of other rhodopsins. We performed femtosecond time-resolved absorption measurements of two HeRs, HeR 48C12 and HeR from Thermoplasmatales archaeon SG8-52-1. Both HeRs exhibit excited-state absorption around 480 nm and stimulated emission in the >650 nm region, and these transient signals decay concomitantly with appearance of photoproduct absorption on a subpicosecond time scale. The observed spectral change indicates that ultrafast retinal photoisomerization proceeds in the femtosecond time region. The transient spectra and dynamics of HeRs are surprisingly similar to those of type-1 rhodopsins, despite remarkable differences in amino acid arrangement in the hydrophobic region of the retinal binding site.

  18. Spectroscopic Study of Proton-Transfer Mechanism of Inward Proton-Pump Rhodopsin, Parvularcula oceani Xenorhodopsin Peer-reviewed

    Keiichi Inoue, Shinya Tahara, Yoshitaka Kato, Satoshi Takeuchi, Tahei Tahara, Hideki Kandori

    The Journal of Physical Chemistry B　122　(25)　6453-6461　2018/06/28

    Publisher: American Chemical Society (ACS)

    DOI： 10.1021/acs.jpcb.8b01279 　

    ISSN： 1520-6106

    eISSN： 1520-5207

  19. Origin of the Reactive and Nonreactive Excited States in the Primary Reaction of Rhodopsins: pH Dependence of Femtosecond Absorption of Light-Driven Sodium Ion Pump Rhodopsin KR2 Peer-reviewed

    Shinya Tahara, Satoshi Takeuchi, Rei Abe-Yoshizumi, Keiichi Inoue, Hiroyuki Ohtani, Hideki Kandori, Tahei Tahara

    The Journal of Physical Chemistry B　122　(18)　4784-4792　2018/05/10

    Publisher: American Chemical Society (ACS)

    DOI： 10.1021/acs.jpcb.8b01934 　

    ISSN： 1520-6106

    eISSN： 1520-5207

  20. Demonstration of a Light-Driven SO42- Transporter and Its Spectroscopic Characteristics Peer-reviewed

    Akiko Niho, Susumu Yoshizawa, Takashi Tsukamoto, Marie Kurihara, Shinya Tahara, Yu Nakajima, Misao Mizuno, Hikaru Kuramochi, Tahei Tahara, Yasuhisa Mizutani, Yuki Sudo

    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY　139　(12)　4376-4389　2017/03

    DOI： 10.1021/jacs.6b12139 　

    ISSN： 0002-7863

  21. Ultrafast Photoreaction Dynamics of a Light-Driven Sodium-Ion-Pumping Retinal Protein from Krokinobacter eikastus Revealed by Femtosecond Time-Resolved Absorption Spectroscopy Peer-reviewed

    Shinya Tahara, Satoshi Takeuchi, Rei Abe-Yoshizumi, Keiichi Inoue, Hiroyuki Ohtani, Hideki Kandori, Tahei Tahara

    JOURNAL OF PHYSICAL CHEMISTRY LETTERS　6　(22)　4481-4486　2015/11

    DOI： 10.1021/acs.jpclett.5b01994 　

    ISSN： 1948-7185

  22. pH-Dependent Photoreaction Pathway of the All-Trans Form of Anabaena Sensory Rhodopsin Peer-reviewed

    Shinya Tahara, Yoshitaka Kato, Hideki Kandori, Hiroyuki Ohtani

    JOURNAL OF PHYSICAL CHEMISTRY B　117　(7)　2053-2060　2013/02

    DOI： 10.1021/jp311217a 　

    ISSN： 1520-6106

Show all ︎Show first 5

Misc. 3

  1. 酸化促進性の獲得からみた SOD1 の毒性発現機構 Invited

    田原進也, 中林孝和

    ファルマシア　60　(5)　398-403　2024/05

  2. 注目の論文「細胞内のありのままの核酸を観る」 Invited

    田原進也

    月刊化学　78　58-59　2023/05

  3. Vibrational Wavepacket Motion in Ultrafast Cyanine Photoisomerization Revealed by Femtosecond Stimulated Raman Spectroscopy Peer-reviewed

    Shinya Tahara, Satoshi Takeuchi, Hiroyuki Ohtani, Tahei Tahara

    International Conference on Ultrafast Phenomena　2016

    Publisher: OSA

    DOI： 10.1364/up.2016.um2a.4 　

Presentations 35

  1. Elucidating the control mechanism of protein liquid-liquid phase separation by Raman microscopy Invited

    Shinya Tahara

    令和7年度化学系学協会東北大会　2025/09/07

  2. ラマン顕微鏡によるタンパク質の液-液相分離と凝集の解析: 疾患発症から薬剤作用まで Invited

    田原進也

    ISSP ワークショップ 「先端的分光計測・化学イメージングが 描き出す、次世代化学研究」　2025/09/05

  3. RNAや薬剤による相分離タンパク質の凝集抑制作用の定量的ラマン顕微解析 Invited

    田原進也

    第12回物理・分析系若手研究者セミナー　2024/11/09

  4. Raman microscopic analyses revealed how a drug and RNAs interact with phase-separated proteins Invited

    Shinya Tahara

    IPR seminar “Toward establishing LLPS research systems”　2024/09/24

  5. 先端的顕微分光法による液-液相分離したタンパク質のダイナミクス解析 Invited

    田原進也

    第46回日本光医学・光生物学会　2024/07/07

  6. RNAによるALS関連タンパク質液滴の凝集抑制効果

    Taisei Ogura, Uchu Matsuura, Shinya Tahara, Shinji Kajimoto, Takakazu Nakabayashi

    日本薬学会第144年会　2024/03/28

  7. ラマン顕微鏡を用いた細胞内超硫黄分子のラベルフリー検出

    古賀 圭祐, 梶本 真司, 田原 進也, 金野 智浩, 中林 孝和

    2023年度 生物物理学会北海道支部-東北支部合同例会　2024/03/22

  8. Near-infrared Raman observation of the tight junction protein ZO-1 LLPS droplets controlled by mechanical stress

    Kaichi Nagai, Shinji Kajimoto, Shinya Tahara, Sayuki Hirano, Noriyuki Kinoshita, Naoto Ueno, Takakazu Nakabayashi

    第17回分子科学討論会　2023/09/15

  9. Development of a highly sensitive Raman spectroscopic method for proteins in aqueous solution using liquid-liquid phase separation

    Ayaka Saito, Reona Tobita, Lisa Kageyama, Shinya Tahara, Shinji Kajimoto, Takakazu Nakabayasi

    第17回分子科学討論会　2023/09/13

  10. Interaction between FUS proteins and RNA in droplets formed via liquid-liquid phase separation detected by Raman microscopy

    Uchu Matsuura, Shinya Tahara, Shinji Kajimoto, Takakazu Nakabayashi

    第17回分子科学討論会　2023/09/12

  11. Developments of a protein condensation method using liquid-liquid phase separation and its application to ultrasensitive Raman detection of proteins in solutions

    Reona Tobita, Shinya Tahara, Shinji Kajimoto, Takakazu Nakabayashi

    第23回日本蛋白質科学会年会　2023/07/05

  12. Improving the efficiency of PET depolymerization by liquid-liquid phase separation of enzymes

    Ippei Suzuki, Shinya Tahara, Takakazu Nakabayashi

    第23回日本蛋白質科学会年会　2023/07/05

  13. SOD1の超硫黄化による酵素活性制御

    田原進也, 山﨑公介, 中林孝和

    第23回日本蛋白質科学会年会　2023/07/05

  14. 自家蛍光寿命イメージングによる液-液相分離したataxin-3の構造変化のラベルフリー観測

    田原進也, 松浦宇宙, 梶本真司, 中林孝和

    第45回日本光医学・光生物学会　2023/06/25

  15. Intramolecular disulfide bond switches enzymatic activity of SOD1 Invited

    Shinya Tahara

    第60回日本生物物理学会年会　2022/09/30

  16. 自家蛍光寿命イメージングを用いた相分離液滴のラベルフリー観測：タンパク質の構造変化ダイナミクス計測

    田原進也, 松浦宇宙, 梶本真司, 中林孝和

    第22回日本蛋白質科学会年会　2022/06/09

  17. 先端的分光法によるタンパク質の病原性発現機構の解析 Invited

    田原進也

    日本薬学会東北支部第9回物理・分析若手研究者セミナー　2021/10/16

  18. Label-free autofluorescence lifetime imaging of liquid-liquid phase separation: structural changes of a pathogenic protein

    Uchu Matsuura, Shinya Tahara, Shinji Kajimoto, Takakazu Nakabayashi

    2021/09/19

  19. Metal ion-dependent promotion of aggregation of Ataxin-3: Effects of poly Q chain length

    Naoki OHTANI, Nozomi GOSO, Kunisato KUROI, Shinya TAHARA, Takakazu NAKABAYASHI

    第30回金属の関与する生体関連反応シンポジウム　2021/06/18

  20. Explaining the toxicity of SOD1 oligomers with their oxidative properties

    Kosuke YAMAZAKI, Shinya TAHARA, Kunisato KUROI, Takumi OHYAMA, Takakazu NAKABAYASHI

    第30回金属の関与する生体関連反応シンポジウム　2021/06/18

  21. SOD1オリゴマーの毒性発現機構：酸化促進性獲得との関係

    田原進也, 山﨑公介, 大山拓実, 黒井邦巧, 中林孝和

    第47回生体分子科学討論会　2021/06/04

  22. Triggers of Primary Protein Dynamics in Photoreceptor Proteins Invited

    S. Tahara

    2020/09

  23. Atomic Contacts Drive Ultrafast Helix Motions in Myoglobin International-presentation Invited

    Shinya Tahara

    11th Asian Conference on Ultrafast Phenomena　2020/01/12

  24. フェムト秒紫外誘導ラマン分光法による微⽣物型ロドプシンの超⾼速タンパク質応答の研究 Invited

    田原進也

    ISSPワークショップ 「レチナールタンパク質の光機能発現の物理と化学」　2019/09/06

  25. Atomic Contacts Drive Structual Changes of Myoglobin

    S. Tahara

    19th Time Resolved Vibrational Spectroscopy　2019/09

  26. Universality of Ultrafast Protein Dynamics of Rhodopsins Revealed by Femtosecond Time-Resolved Ultraviolet Stimulated Raman Spectroscopy

    Shinya Tahara

    2019/03/18

  27. Ultrafast Protein Dynamics of Bacteriorhodopsin Revealed by Deep-UV Femtosecond Stimulated Raman spectroscopy International-presentation

    Shinya Tahara

    The 26th International Conference on Raman Spectroscopy　2018/08/29

  28. フェムト秒時間分解深紫外誘導ラマン分光法によるバクテリオロドプシンの超高速タンパク質応答の観測

    田原進也

    第11回分子科学討論会　2017/09/15

  29. フェムト秒過渡吸収のpH依存性によるナ トリウムイオン輸送ロドプシン反応性・非反応性励起状態の起源の解明

    田原進也

    平成29年度日本分光学会年次講演会　2017/05/24

  30. Watching the Excited-State Structural Distribution Dynamics by Femtosecond Stimulated Raman Spectroscopy International-presentation Invited

    Shinya Tahara

    SNU-RIKEN young investigator workshop on nanospectroscopy　2017/01/06

  31. フェムト秒誘導ラマン分光法を用いた無障壁反応における構造分布ダイナミクスの研究 Invited

    田原進也

    若手研究者による先端的レーザー分光シンポジウム　2016/12/03

  32. Vibrational Wavepacket Motion in Ultrafast Cyanine Photoisomerization Revealed by Femtosecond Stimulated Raman Spectroscopy International-presentation

    Shinya Tahara

    2016/07/18

  33. Structural Dynamics of Barrierless Reaction Tracked by Femtosecond Stimulated Raman Spectroscopy International-presentation

    Shinya Tahara

    2016/04/07

  34. Na+ポンプ型ロドプシンKR2 の超高速光反応 Invited

    田原進也

    新学術領域「柔らかな分子系」第 13 回 ワークショップ 「光駆動ナトリウムポンプからタンパク質の柔らかさと 機能のつながりを考える」　2015/10/28

  35. 近赤外フェムト秒誘導ラマン分光法による無障壁反応における構造分布ダイナミクスの観測

    田原進也、竹内佐年、大谷弘之、田原太平

    第9回分子科学討論会　2015/09

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Research Projects 6

  1. 神経変性疾患原因タンパク質の液-液相分離と共凝集の関係

    田原進也

    Category: 薬学系研究助成

    2024/08 - 2029/03

  2. 液-液相分離により生成したタンパク質液滴内における分子間相互作用のラマン顕微解析

    田原進也

    Offer Organization: 日本学術振興会

    Category: 基盤研究(B)

    Institution: 東北大学

    2024/04 - 2028/03

  3. 液-液相分離を用いたプラスチックやバイオマスの高効率分解

    田原進也

    Offer Organization: 加藤記念バイオサイエンス財団

    Category: 研究助成

    2024/04 - 2026/03

  4. 蛍光寿命・異方性顕微分光による相分離液滴中のタンパク質周辺環境のラベルフリー解析

    田原進也

    Offer Organization: 日本学術振興会

    Category: 若手研究

    Institution: 東北大学

    2021/04 - 2023/03

    More details Close

    液-液相分離(LLPS)は均一な高分子溶液が濃度の異なる2つ以上の液相に分離する現象である。細胞内において核酸やタンパク質はLLPSを起こし、高濃度の生体分子を含む液滴を形成する。LLPSは生体反応制御に重要な役割を担うが、タンパク質の凝集を促進し、神経変性疾患等の原因となることも分かってきた。LLPSにより生成した液滴内部のタンパク質の物性や構造の理解は、生体反応制御や疾患発症機構の理解に重要である。本研究では液滴内部のタンパク質の構造を蛍光標識等を用いずに調べる手法として、自家蛍光寿命イメージングを提案する。 令和3年度は、紫外励起蛍光寿命イメージング装置を構築し、マチャドジョセフ病原因タンパク質ataxin-3のLLPS液滴の自家蛍光イメージングおよび寿命測定を実施した。Ataxin-3のトリプトファン(Trp)残基の蛍光を検出し、液滴の無標識観測に成功した。またTrpの蛍光寿命を観測することにより、水溶液中および液滴内におけるataxin-3周辺の疎水性の違いを検出した。さらにataxin-3の液滴は蛍光寿命の経時変化を示した。この変化からataxin-3は液滴内で多段階的に変性することが明らかとなった。以上のようにLLPS液滴内部のタンパク質構造変化を無標識で観測することに初めて成功した。Ataxin-3の凝集がマチャドジョセフ病の原因となることが示唆されていることから、本研究で得られた知見は本疾患の発症機構を解明するための重要な手がかりとなる。 さらに本手法を筋萎縮性側索硬化症関連タンパク質Fused in sarcoma (FUS)に適用したところ、LLPSによりFUSを構成するチロシン(Tyr)の蛍光寿命が変化した。これは液滴内におけるFUS分子間の特異な相互作用を反映していると考えられ、現在はその詳細を明らかにするための実験を行っている。

  5. 光異性化に先立つタンパク質構造変化の誘起機構の解明 Competitive

    田原進也

    Offer Organization: 日本学術振興会

    System: 若手研究

    2019/04 - 2021/03

  6. 時間分解紫外共鳴ラマン分光法によるUV-B光受容タンパク質の光反応研究 Competitive

    田原進也

    Offer Organization: 日本学術振興会

    System: 特別研究員奨励費

    2018/04 - 2021/03

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Teaching Experience 4

  1. 構造化学　Tohoku University, Faculty of Pharmaceutical Sciences

  2. 構造薬学実習　Tohoku University

  3. 自然科学総合実験　東北大学工学部

  4. 自然科学総合実験　東北大学工学部