研究者データベース

能代 大輔(ノシロ ダイスケ)
遺伝子病制御研究所 疾患制御研究部門
特任助教

基本情報

所属

  • 遺伝子病制御研究所 疾患制御研究部門

職名

  • 特任助教

学位

  • 博士(薬学)(2012年03月 京都大学)

科研費研究者番号

  • 90751107

ORCID ID

J-Global ID

研究キーワード

  • リポソーム   天然変性タンパク質   液液相分離   タンパク質科学   オートファジー   電気生理学   高速原子間力顕微鏡   

研究分野

  • ライフサイエンス / 薬系分析、物理化学 / イメージング

職歴

  • 2022年04月 - 現在 北海道大学 遺伝子病制御研究所 特任助教
  • 2018年04月 - 2022年03月 公益財団法人微生物化学研究会微生物化学研究所 博士研究員
  • 2017年10月 - 2018年03月 金沢大学ナノ生命科学研究所 博士研究員
  • 2013年10月 - 2017年09月 金沢大学バイオAFM先端研究センター 博士研究員
  • 2012年10月 - 2013年09月 オックスフォード大学 博士研究員
  • 2012年04月 - 2012年09月 京都大学化学研究所 博士研究員

学歴

  • 2009年04月 - 2012年03月   京都大学大学院   薬学研究科   生命薬科学
  • 2007年04月 - 2009年03月   京都大学大学院   薬学研究科   生命薬科学
  • 2003年04月 - 2007年03月   京都大学   薬学部   総合薬学科

所属学協会

  • 日本生化学会   日本生物物理学会   日本薬学会   

研究活動情報

論文

  • Mirai Tanigawa, Katsuyoshi Yamamoto, Satoru Nagatoishi, Koji Nagata, Daisuke Noshiro, Nobuo N. Noda, Kouhei Tsumoto, Tatsuya Maeda
    Communications Biology 4 1 2021年09月 [査読有り]
     
    AbstractTOR complex 1 (TORC1) is an evolutionarily-conserved protein kinase that controls cell growth and metabolism in response to nutrients, particularly amino acids. In mammals, several amino acid sensors have been identified that converge on the multi-layered machinery regulating Rag GTPases to trigger TORC1 activation; however, these sensors are not conserved in many other organisms including yeast. Previously, we reported that glutamine activates yeast TORC1 via a Gtr (Rag ortholog)-independent mechanism involving the vacuolar protein Pib2, although the identity of the supposed glutamine sensor and the exact TORC1 activation mechanism remain unclear. In this study, we successfully reconstituted glutamine-responsive TORC1 activation in vitro using only purified Pib2 and TORC1. In addition, we found that glutamine specifically induced a change in the folding state of Pib2. These findings indicate that Pib2 is a glutamine sensor that directly activates TORC1, providing a new model for the metabolic control of cells.
  • Noriyuki Kodera, Daisuke Noshiro, Sujit K. Dora, Tetsuya Mori, Johnny Habchi, David Blocquel, Antoine Gruet, Marion Dosnon, Edoardo Salladini, Christophe Bignon, Yuko Fujioka, Takashi Oda, Nobuo N. Noda, Mamoru Sato, Marina Lotti, Mineyuki Mizuguchi, Sonia Longhi, Toshio Ando
    Nature Nanotechnology 16 2 181 - 189 2021年02月 [査読有り]
  • Shun Kageyama, Sigurdur Runar Gudmundsson, Yu-Shin Sou, Yoshinobu Ichimura, Naoki Tamura, Saiko Kazuno, Takashi Ueno, Yoshiki Miura, Daisuke Noshiro, Manabu Abe, Tsunehiro Mizushima, Nobuaki Miura, Shujiro Okuda, Hozumi Motohashi, Jin-A Lee, Kenji Sakimura, Tomoyuki Ohe, Nobuo N. Noda, Satoshi Waguri, Eeva-Liisa Eskelinen, Masaaki Komatsu
    Nature Communications 12 1 2021年01月 [査読有り]
     
    AbstractAutophagy contributes to the selective degradation of liquid droplets, including the P-Granule, Ape1-complex and p62/SQSTM1-body, although the molecular mechanisms and physiological relevance of selective degradation remain unclear. In this report, we describe the properties of endogenous p62-bodies, the effect of autophagosome biogenesis on these bodies, and the in vivo significance of their turnover. p62-bodies are low-liquidity gels containing ubiquitin and core autophagy-related proteins. Multiple autophagosomes form on the p62-gels, and the interaction of autophagosome-localizing Atg8-proteins with p62 directs autophagosome formation toward the p62-gel. Keap1 also reversibly translocates to the p62-gels in a p62-binding dependent fashion to activate the transcription factor Nrf2. Mice deficient for Atg8-interaction-dependent selective autophagy show that impaired turnover of p62-gels leads to Nrf2 hyperactivation in vivo. These results indicate that p62-gels are not simple substrates for autophagy but serve as platforms for both autophagosome formation and anti-oxidative stress.
  • Kazuaki Matoba, Tetsuya Kotani, Akihisa Tsutsumi, Takuma Tsuji, Takaharu Mori, Daisuke Noshiro, Yuji Sugita, Norimichi Nomura, So Iwata, Yoshinori Ohsumi, Toyoshi Fujimoto, Hitoshi Nakatogawa, Masahide Kikkawa, Nobuo N Noda
    Nature structural & molecular biology 27 12 1209 - 1209 2020年12月 
    An amendment to this paper has been published and can be accessed via a link at the top of the paper.
  • Kazuaki Matoba, Tetsuya Kotani, Akihisa Tsutsumi, Takuma Tsuji, Takaharu Mori, Daisuke Noshiro, Yuji Sugita, Norimichi Nomura, So Iwata, Yoshinori Ohsumi, Toyoshi Fujimoto, Hitoshi Nakatogawa, Masahide Kikkawa, Nobuo N Noda
    Nature structural & molecular biology 27 12 1185 - 1193 2020年12月 [査読有り]
     
    The molecular function of Atg9, the sole transmembrane protein in the autophagosome-forming machinery, remains unknown. Atg9 colocalizes with Atg2 at the expanding edge of the isolation membrane (IM), where Atg2 receives phospholipids from the endoplasmic reticulum (ER). Here we report that yeast and human Atg9 are lipid scramblases that translocate phospholipids between outer and inner leaflets of liposomes in vitro. Cryo-EM of fission yeast Atg9 reveals a homotrimer, with two connected pores forming a path between the two membrane leaflets: one pore, located at a protomer, opens laterally to the cytoplasmic leaflet; the other, at the trimer center, traverses the membrane vertically. Mutation of residues lining the pores impaired IM expansion and autophagy activity in yeast and abolished Atg9's ability to transport phospholipids between liposome leaflets. These results suggest that phospholipids delivered by Atg2 are translocated from the cytoplasmic to the luminal leaflet by Atg9, thereby driving autophagosomal membrane expansion.
  • Yuki Kawasaki, Hirotaka Ariyama, Hajime Motomura, Daisuke Fujinami, Daisuke Noshiro, Toshio Ando, Daisuke Kohda
    Journal of Molecular Biology 432 22 5951 - 5965 2020年11月 [査読有り]
     
    Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains. Using high-speed atomic force microscopy (AFM), we investigated the dynamic properties of OST molecules embedded in biomembranes. An archaeal single-subunit OST protein was immobilized on a mica support via biotin-avidin interactions and reconstituted in a lipid bilayer. The distance between the top of the protein molecule and the upper surface of the lipid bilayer was monitored in real-time. The height of the extramembranous part exhibited a two-step variation with a difference of 1.8 nm. The high and low states are designated as state 1 and state 2, respectively. The transition processes between the two states fit well to single exponential functions, suggesting that the observed dynamic exchange is an intrinsic property of the archaeal OST protein. The two sets of cross peaks in the NMR spectra of the protein supported the conformational changes between the two states in detergent-solubilized conditions. Considering the height values measured in the AFM measurements, state 1 is closer to the crystal structure, and state 2 has a more compact form. Subsequent AFM experiments indicated that the binding of the sugar donor LLO decreased the structural fluctuation and shifted the equilibrium almost completely to state 1. This dynamic behavior is likely necessary for efficient catalytic turnover. Presumably, state 2 facilitates the immediate release of the bulky glycosylated polypeptide product, thus allowing OST to quickly prepare for the next catalytic cycle.
  • Akinori Yamasaki, Jahangir Md Alam, Daisuke Noshiro, Eri Hirata, Yuko Fujioka, Kuninori Suzuki, Yoshinori Ohsumi, Nobuo N Noda
    Molecular cell 77 6 1163 - 1175 2020年03月19日 [査読有り][通常論文]
     
    Clearance of biomolecular condensates by selective autophagy is thought to play a crucial role in cellular homeostasis. However, the mechanism underlying selective autophagy of condensates and whether liquidity determines a condensate's susceptibility to degradation by autophagy remain unknown. Here, we show that the selective autophagic cargo aminopeptidase I (Ape1) undergoes phase separation to form semi-liquid droplets. The Ape1-specific receptor protein Atg19 localizes to the surface of Ape1 droplets both in vitro and in vivo, with the "floatability" of Atg19 preventing its penetration into droplets. In vitro reconstitution experiments reveal that Atg19 and lipidated Atg8 are necessary and sufficient for selective sequestration of Ape1 droplets by membranes. This sequestration is impaired by mutational solidification of Ape1 droplets or diminished ability of Atg19 to float. Taken together, we propose that cargo liquidity and the presence of sufficient amounts of autophagic receptor on cargo are crucial for selective autophagy of biomolecular condensates.
  • Yuko Fujioka, Jahangir Md Alam, Daisuke Noshiro, Kazunari Mouri, Toshio Ando, Yasushi Okada, Alexander I May, Roland L Knorr, Kuninori Suzuki, Yoshinori Ohsumi, Nobuo N Noda
    Nature 578 7794 301 - 305 2020年02月 [査読有り][通常論文]
     
    Many biomolecules undergo liquid-liquid phase separation to form liquid-like condensates that mediate diverse cellular functions1,2. Autophagy is able to degrade such condensates using autophagosomes-double-membrane structures that are synthesized de novo at the pre-autophagosomal structure (PAS) in yeast3-5. Whereas Atg proteins that associate with the PAS have been characterized, the physicochemical and functional properties of the PAS remain unclear owing to its small size and fragility. Here we show that the PAS is in fact a liquid-like condensate of Atg proteins. The autophagy-initiating Atg1 complex undergoes phase separation to form liquid droplets in vitro, and point mutations or phosphorylation that inhibit phase separation impair PAS formation in vivo. In vitro experiments show that Atg1-complex droplets can be tethered to membranes via specific protein-protein interactions, explaining the vacuolar membrane localization of the PAS in vivo. We propose that phase separation has a critical, active role in autophagy, whereby it organizes the autophagy machinery at the PAS.
  • Sone E, Noshiro D, Ikebuchi Y, Nakagawa M, Khan M, Tamura Y, Ikeda M, Oki M, Murali R, Fujimori T, Yoda T, Honma M, Suzuki H, Ando T, Aoki K
    Biochemical and biophysical research communications 509 2 435 - 440 2019年02月 [査読有り][通常論文]
     
    We recently found that the membrane-bound receptor activator of NF-kappa B ligand (RANKL) on osteoblasts works as a receptor to stimulate osteoblast differentiation, however, the reason why the RANKL-binding molecules stimulate osteoblast differentiation has not been well clarified. Since the induction of cell surface receptor clustering is known to lead to cell activation, we hypothesized that the induction of membrane-RANKL clustering on osteoblasts might stimulate osteoblast differentiation. lmmunoblotting showed that the amount of RANKL on the membrane was increased by the RANKL-binding peptide OP3-4, but not by osteoprotegerin (OPG), the other RANKL-binding molecule, in Gfp-Rankl-transfected ST2 cells. Observation under a high-speed atomic force microscope (HS-AFM) revealed that RANKL molecules have the ability to form clusters. The induction of membrane-RANKL-OPG-Fc complex clustering by the addition of IgM in Gfp-Rankl-transfected ST2 cells could enhance the expression of early markers of osteoblast differentiation to the same extent as OP3-4, while OPG-Fc alone could not. These results suggest that the clustering-formation of membrane-RANKL on osteoblasts could stimulate early osteoblast differentiation. (C) 2018 Elsevier Inc. All rights reserved.
  • Daisuke Noshiro, Toshio Ando
    Philosophical Transactions of the Royal Society B: Biological Sciences 373 1749 2018年06月19日 [査読有り][通常論文]
     
    A double-ring-shaped tetradecameric GroEL complex assists proper protein folding in cooperation with the cochaperonin GroES. The dynamic GroEL– GroES interaction reflects the allosteric intra- and inter-ring communications and the chaperonin reaction. Therefore, revealing this dynamic interaction is essential to understanding the allosteric communications and the operation mechanism of GroEL. Nevertheless, how this interaction proceeds in the chaperonin cycle has long been controversial. Here, we directly image the dynamic GroEL–GroES interaction under conditions with and without foldable substrate protein using high-speed atomic force microscopy. Then, the imaging results obtained under these conditions and our previous results in the presence of unfoldable substrate are compared. The molecular movies reveal that the entire reaction pathway is highly complicated but basically identical irrespective of the substrate condition. A prominent (but moderate) difference is in the population distribution of intermediate species: symmetric GroEL: GroES2 and asymmetric GroEL: GroES1 complexes, and GroES– unbound GroEL. This difference is mainly attributed to the longer lifetime of GroEL: GroES1 complexes in the presence of foldable substrate. Moreover, the inter-ring communication, which is the basis for the alternating action of the two rings, occurs at two distinct (GroES association and dissociation) steps in the main reaction pathway, irrespective of the substrate condition. This article is part of a discussion meeting issue ‘Allostery and molecular machines’.
  • Akihiko Oku, Miki Imanishi, Daisuke Noshiro, Tomo Murayama, Toshihide Takeuchi, Ikuhiko Nakase, Shiroh Futaki
    BIOPOLYMERS 108 1 2017年01月 [査読有り][通常論文]
     
    Calmodulin is a representative calcium-binding protein comprised of four Ca2+-binding motifs with a helix-loop-helix structure (EF-hands). In this study, we clarified the potential of peptide segments derived from the third and fourth EF-hands (EF3 and EF4) to act as recognition tags. Through an analysis of the mode of disulfide formation among cysteines inserted at the N- or C-terminus of these peptide segments, EF3 and EF4 peptides were suggested to form a heterodimer with a topology similar to that in the wild-type protein. Heterodimer formation was shown to be a function of the Ca2+ concentration, suggesting that these structures may be used as Ca2+-switchable recognition tags. An example of an "EF-tag" system involving the membrane fusion of liposomes decorated with EF3 and EF4 peptides is presented.
  • Hayashi Yamamoto, Yuko Fujioka, Sho W. Suzuki, Daisuke Noshiro, Hironori Suzuki, Chika Kondo-Kakuta, Yayoi Kimura, Hisashi Hirano, Toshio Ando, Nobuo N. Noda, Yoshinori Ohsumi
    DEVELOPMENTAL CELL 38 1 86 - 99 2016年07月 [査読有り][通常論文]
     
    Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 subcomplex) are initially engaged. However, the molecular mechanisms underlying the multimeric assembly of these complexes remain unclear. Using structural and biological techniques, we herein demonstrate that Atg13 has a large intrinsically disordered region (IDR) and interacts with two distinct Atg17 molecules using two binding regions in the IDR. We further reveal that these two binding regions are essential not only for Atg1 complex assembly in vitro, but also for PAS organization in vivo. These findings underscore the structural and functional significance of the IDR of Atg13 in autophagy initiation: Atg13 provides intercomplex linkages between Atg17-Atg29-Atg31 complexes, thereby leading to supramolecular self-assembly of Atg1 complexes, in turn accelerating the initial events of autophagy, including autophosphorylation of Atg1, recruitment of Atg9 vesicles, and phosphorylation of Atg9 by Atg1.
  • Shiroh Futaki, Daisuke Noshiro, Tatsuto Kiwada, Koji Asami
    Accounts of Chemical Research 46 12 2924 - 2933 2013年12月17日 [査読有り][通常論文]
     
    Ion channels allow the influx and efflux of specific ions through a plasmamembrane. Many ion channels can sense, for example, the membrane potential (the voltage gaps between the inside and the outside of the membrane), specific ligands such as neurotransmitters, and mechanical tension within the membrane. They modulate cell function in response to these stimuli. Researchers have focused on developing peptide- and non-peptide-based model systems to elucidate ion-channel protein functions and to create artificial sensing systems.In this Account, we employed a typical peptide that forms ion channels,alamethicin, as a model to evaluate our methodologies for controlling the assembly states of channel-forming molecules in membranes. As alamethicin self-assembles in membranes, it prompts channel formation, but number of peptide molecules in these channels is not constant. Using planar-lipid bilayer methods, we monitored the association states of alamethicin in real time.Many ligand-gated, natural-ion channel proteins have large extramembranedomains. As these proteins interact with specific ligands, those conformational alterations in the extramembrane domains are transmitted to the transmembrane, pore-forming domains to open and close the channels. We hypothesized that if we conjugated suitable extramembrane segments to alamethicin, ligand binding to the extramembrane segments could alter the structure of the extramembrane domains and influence the association states or association numbers of alamethicin in the membranes. We could then assess those changes by using single-channel current recording. We found that we could modulate channel assembly and eventual ion flux with attached leucine-zipper extramembrane peptide segments. Using conformationally switchable leucine-zipper extramembrane segments that respond to Fe 3+, we fabricated an artificial Fe3+-sensitive ion channel a decrease in the helical content of the extramembrane segment led to an increase in the channel current.When we added a calmodulin C-terminus segment, we formed a channel that was sensitive to Ca2+. This result demonstrated that we could prepare artificial channels that were sensitive to specific ligands by adding appropriate extramembrane segments from natural protein motifs that respond to external stimuli.In conclusion, our research points to the possibility of creating tailored sensor or signal transduction systems through the conjugation of a conformationally switchable extramembrane peptide/protein segment to a suitable transmembrane peptide segment. © 2013 American Chemical Society.
  • Daisuke Noshiro, Kazuhiro Sonomura, Hao-Hsin Yu, Miki Imanishi, Koji Asami, Shiroh Futaki
    Bioconjugate Chemistry 24 2 188 - 195 2013年02月20日 [査読有り][通常論文]
     
    Using native chemical ligation, we constructed a Ca2+-gated fusion channel protein consisting of alamethicin and the C-terminal domain of calmodulin. At pH 5.4 and in the absence of Ca2+, this fusion protein yielded a burst-like channel current with no discrete channel conductance levels. However, Ca2+ significantly lengthened the specific channel open state and increased the mean channel current, while Mg2+ produced no significant changes in the channel current. On the basis of 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescent measurement, Ca 2+-stimulated gating may be related to an increased surface hydrophobicity of the extramembrane segment of the fusion protein. © 2012 American Chemical Society.
  • Daisuke Noshiro, Koji Asami, Shiroh Futaki
    BIOORGANIC & MEDICINAL CHEMISTRY 20 23 6870 - 6876 2012年12月 [査読有り][通常論文]
     
    Alamethicin (Alm), an antimicrobial peptide rich in alpha-aminoisobutyric acid (Aib), is known to self-assemble to form channels in the membranes. Previously, we reported that HG-Alm, an Alm analog with a single His residue at the N-terminus, forms channel assemblies with extremely long lifetimes in the presence of Zn2+. In this study, HG-Alm analogs, in the sequences of which all Aib residues were substituted by Leu, norvaline (Nva), or norleucine (Nle), were synthesized and their leakage activities were measured using fluorescent dye-loaded liposomes. We found that these peptides could be categorized into two classes with different gating responses to Zn2+. (C) 2012 Elsevier Ltd. All rights reserved.
  • Miki Imanishi, Tomohiro Nakaya, Tatsuya Morisaki, Daisuke Noshiro, Shiroh Futaki, Yukio Sugiura
    CHEMBIOCHEM 11 12 1653 - 1655 2010年08月 [査読有り][通常論文]
  • Daisuke Noshiro, Koji Asami, Shiroh Futaki
    BIOPHYSICAL JOURNAL 98 9 1801 - 1808 2010年05月 [査読有り][通常論文]
     
    Alamethicin, a member of the peptaibol family of antibiotics, is a typical channel-forming peptide with a helical structure. The self-assembly of the peptide in the membranes yields voltage-dependent channels. In this study, three alamethicin analogs possessing a charged residue (His, Lys, or Glu) on their N-termini were designed with the expectation of stabilizing the transmembrane structure. A slight elongation of channel lifetime was observed for the Lys and Glu analogs. On the other hand, extensive stabilization of certain channel open states was observed for the His analog. This stabilization was predominantly observed in the presence of metal ions such as Zn(2+), suggesting that metal coordination with His facilitates the formation of a supramolecular assembly in the membranes. Channel stability was greatly diminished by acetylation of the N-terminal amino group, indicating that the N-terminal amino group also plays an important role in metal coordination.
  • Daisuke Noshiro, Koji Asami, Shiroh Futaki
    YAKUGAKU ZASSHI-JOURNAL OF THE PHARMACEUTICAL SOCIETY OF JAPAN 128 41 - 41 2008年 [査読有り][通常論文]

その他活動・業績

  • 能代 大輔, 野田 展生 実験医学 39 (13) 2046 -2051 2021年08月 
    液-液相分離はその生物学的な重要性が認識されはじめて久しいが、選択的オートファジーにおいても重大な役割を担っている。選択的オートファジーは、液-液相分離により液滴状態となったタンパク質を分解対象のひとつとしており、その際は液滴の適度な液体度と、レセプターを介した液滴-隔離膜間相互作用が重要な役割を担う。本稿では、p62液滴、ストレス顆粒、そしてエンドサイトーシス異常の際に形成されるEND液滴の例を紹介するとともに、液滴選択的オートファジーのメカニズムを議論する。(著者抄録)
  • 山崎章徳, 山崎章徳, ALAM Jahangir MD., 能代大輔, 平田恵理, 藤岡優子, MAY Alexander I., 鈴木邦律, 鈴木邦律, 鈴木邦律, 大隅良典, 野田展生 日本細胞生物学会大会(Web) 73rd 2021年
  • 谷川美頼, 山本勝良, 長門石曉, 津本浩平, 能代大輔, 野田展生, 永田宏次, 前田達哉, 前田達哉 日本農芸化学会大会講演要旨集(Web) 2021 2021年
  • 蔭山俊, GUDMUNDSSON Sigurdur, SOU Yu-Shin, 一村義信, 田村直輝, 數野彩子, 上野隆, 三浦芳樹, 能代大輔, 阿部学, 水島恒裕, 三浦信明, 奥田修二郎, 本橋ほづみ, LEE Jin-A, 崎村建司, 大江知之, 野田展生, 和栗聡, ESKELINEN Eeva-Liisa, 小松雅明 日本細胞生物学会大会(Web) 73rd 2021年
  • マルチモードオートファジー カーゴの液体度が選択的オートファジーでの取り込みを左右する(Liquidty is a critical determinant for selective autophagy of protein condensates)
    山崎 章徳, Alam Jahangir, 能代 大輔, 平田 恵理, 藤岡 優子, 鈴木 邦律, 大隅 良典, 野田 展生 日本細胞生物学会大会講演要旨集 72回 S9 -4 2020年06月
  • 能代 大輔, 野田 展生 実験医学 38 (5) 750 -755 2020年03月 
    タンパク質や核酸がLLPSすることで形成される液滴は、時間経過やストレス、変異等で固体化が進みゲルや凝集体となる。オートファジーは液滴を選択的に分解するが、効率的分解には液滴の適度な固体化が重要なようである。またLLPSはオートファジー関連因子の集積を通してオートファジーのマシーナリーの制御も担う。高速AFMは液滴の構造解析に適しており、同じタンパク質に関して液滴状態とゲル状態の構造的差異を見分けることが可能である。(著者抄録)
  • 谷川美頼, 山本勝良, 長門石曉, 永田宏次, 能代大輔, 野田展生, 津本浩平, 津本浩平, 前田達哉, 前田達哉 日本分子生物学会年会プログラム・要旨集(Web) 43rd 2020年
  • 川崎由貴, 有山弘高, 藤浪大輔, 本村肇, SRIVASTAVA Ashutosh, TAMA Florence, 能代大輔, 安藤敏夫, 真柳浩太, 神田大輔 日本糖質学会年会要旨集 38th 2019年
  • 山崎章徳, ALAM Jahangir Md., 能代大輔, 野田展生 日本細胞生物学会大会(Web) 71st 2019年
  • オートファジーの足場タンパク質Atg17-Atg29-Atg31複合体の高速AFM観察
    能代 大輔, 藤岡 優子, 野田 展生, 安藤 敏夫 日本生化学会大会プログラム・講演要旨集 91回 [2P -003] 2018年09月 [査読無し][通常論文]
  • 曽根絵梨, MASUD Khan, 能代大輔, 池淵祐樹, 本間雅, 田村幸彦, 菅森泰隆, 鈴木洋史, 宇田川信之, 青木和広 日本骨形態計測学会雑誌 28 (2) 2018年
  • 実験・シミュレーション・データ科学の融合による遺伝情報分子システムの生物物理 高速AFMによる天然変性タンパク質の構造動態解析(Biophysics of genetic information molecules and systems: Integrated approach of experiments, simulations, and data science Structural dynamics analysis of intrinsically disordered proteins by high-speed AFM)
    Kodera Noriyuki, Noshiro Daisuke, Dora Sujit, Ando Toshio 生物物理 57 (Suppl.1-2) S191 -S191 2017年08月 [査読無し][通常論文]
  • ビオチン化した生体分子の迅速簡便な固定化法のための、タマビジン2の二次元結晶(Two-dimensional crystals of tamavidin 2 for a quick and easy method of immobilization of biotinylated biomolecules)
    Noshiro Daisuke, Kodera Noriyuki, Ando Toshio 生物物理 57 (Suppl.1-2) S268 -S268 2017年08月 [査読無し][通常論文]
  • 味覚受容体細胞外領域ヘテロ二量体の発現・精製および性状解析(Expression, purification, and characterization of the entire heterodimeric extracellular regions of fish taste receptor)
    Maruhashi Hiroki, Noshiro Daisuke, Yasui Norihisa, Ando Toshio, Yamashita Atsuko 生物物理 57 (Suppl.1-2) S313 -S313 2017年08月 [査読無し][通常論文]
  • 高速AFMによる古細菌S.solfataricus由来ミニ染色体維持(ssoMCM)タンパク質複合体の観察(Observation of S. solfataricus archaeal minichromosome maintenance(ssoMCM) protein complex by high-speed AFM)
    Noshiro Daisuke, Kodera Noriyuki, Ando Toshio 生物物理 56 (Suppl.1-2) S276 -S276 2016年10月 [査読無し][通常論文]
  • 能代 大輔 ファルマシア 52 (9) 881 -881 2016年 [査読無し][通常論文]
     
    バクテリアマイクロコンパートメント(bacterial microcompart‐ment:BMC)は,正二十面体様のタンパク質の殻によって形成される,広く細菌類にみられるオルガネラである.内部に炭素固定に関連する重要な酵素類を含むカルボキシソームは,その代表例である.空間を区画化することで目的の反応に必要な酵素類の濃度を高め,反応を阻害する外部の要因から防御する役割を持つため,BMCは効率よく反応を行うナノリアクターとしての応用価値も見いだされている.BMCの殻の小平面は,主に単一の六量体形成シェルタンパク質BMC-Hにより形成されているが,シェルタンパク質がどのように自己集合して高次構造を形成するのかは未解明のままである.一方,高速AFM(high-speed atomic force microscopy:HS-AFM)は,生理的条件下に近い水溶液中でのタンパク質の動的挙動をリアルタイムで直接観察することが可能な装置である.これまでにアクチン上でのミオシンVの歩行運動や,回転軸を除いたF1-ATPaseの回転運動,バクテリオロドプシンの光励起による構造変化などの観察が行われた.最近Sutterらにより,高速AFMを用いて,BMC-H六量体の自己集合ダイナミクスが初めて観察されたので,本稿で紹介する.
    なお,本稿は下記の文献に基づいて,その研究成果を紹介するものである.
    1) Chowdhury C. et al., Microbiol. Mol. Biol. Rev., 78, 438-468 (2014).
    2) Frank S. et al., J. Biotechnol., 163, 273-279 (2013).
    3) Ando T. et al., Annu. Rev. Biophys., 42, 393-414 (2013).
    4) Sutter M. et al., Nano Lett., 16, 1590-1595 (2016).
  • NOSHIRO Daisuke, SONOMURA Kazuhiro, YU Hao-Hsin, IMANISHI Miki, ASAMI Koji, FUTAKI Shiroh Peptide science : proceedings of the ... Japanese Peptide Symposium 2012 183 -184 2013年03月01日 [査読無し][通常論文]
  • R. Kawano, D. Noshiro, T. Osaki, T. Osaki, K. Kamiya, K. Asami, S. Futaki, S. Takeuchi, S. Takeuchi 17th International Conference on Miniaturized Systems for Chemistry and Life Sciences, MicroTAS 2013 1 32 -34 2013年01月01日 [査読無し][通常論文]
     
    This paper describes the electrical detection of single-stranded DNA (ssDNA) at the single molecule level using an engineered alamethicin (Aim) channel embedded in bilayer lipid membranes (BLMs). Nanopore sequencing has the potential to become a direct, fast and inexpensive DNA sequencing methodology (Fig. 1). We propose here the chemically covalent dimmers of Aim (di-Alm) in which monomers were linked at their N-terminal ends and the di-Alm forms mainly the 6-mers (1.3 nm dia.). In addition, the conductance states were stabilized with lifetimes up to 200-fold longer than the same sates observed with monomers. Using the di-Alm nanopore, we can observe the slow ssDNA translocation and this finding highlight the importance of the di-Alm in the future ofj nanopore sequencing. Copyright © (2013) by the Chemical and Biological Microsystems Society All rights reserved.
  • リポソーム内物質のリーケージを金属により制御可能なチャネルペプチドの創製
    能代大輔, 浅見耕司, 二木史朗 日本ケミカルバイオロジー学会 第7回年会 ,京都(京都大学百周年時計台記念館) 2012年06月08日 [査読無し][通常論文]
  • Design and Creation of a Ca2+-sensitive Artificial Channel Protein
    NOSHIRO, Daisuke, SONOMURA, Kazuhiro, Yu H.H, IMANISHI, Miki, ASAMI, Kouji, FUTAKI, Shiroh International Symposium on Innovative Nanobiodevices ISIN 2012 ,Nagoya, Japan 2012年03月21日 [査読無し][通常論文]
  • NOSHIRO Daisuke, ASAMI Koji, FUTAKI Shiroh Peptide science : proceedings of the ... Japanese Peptide Symposium 2011 189 -190 2012年03月01日 [査読無し][通常論文]
  • ヒスチジン含有アラメチシン誘導体を用いた金属イオンによるリーケージ制御
    能代大輔, 浅見耕司, 二木史朗 第48回ペプチド討論会 ,札幌(札幌コンベンションセンター) 2011年09月27日 [査読無し][通常論文]
  • 新規アラメチシン誘導体による金属を用いたリーケージ制御
    能代大輔, 浅見耕司, 二木史朗 第5回バイオ関連化学シンポジウム ,つくば(つくば国際会議場「エポカルつくば」) 2011年09月13日 [査読無し][通常論文]
  • Alamethicinをベースにした金属イオン感受性人工イオンチャネルの創製
    能代大輔, 浅見耕司, 二木史朗 日本ケミカルバイオロジー学会第6回年会 ,東京(東京工業大学) 2011年05月24日 [査読無し][通常論文]
  • FUTAKI Shiroh, IMANISHI Miki, NAKAYA Tomohiro, MORISAKI Tatsuya, NOSHIRO Daisuke, SUGIURA Yukio Peptide science : proceedings of the ... Japanese Peptide Symposium 2010 16 -16 2011年03月01日 [査読無し][通常論文]
  • NAKAYA Tomohiro, IMANISHI Miki, MORISAKI Tatsuya, NOSHIRO Daisuke, SUGIURA Yukio, FUTAKI Shiroh Peptide science : proceedings of the ... Japanese Peptide Symposium 2010 231 -231 2011年03月01日 [査読無し][通常論文]
  • NOSHIRO Daisuke, ASAMI Koji, FUTAKI Shiroh Peptide science : proceedings of the ... Japanese Peptide Symposium 2010 177 -177 2011年03月01日 [査読無し][通常論文]
  • D. Noshiro, K. Asami, S. Futaki BIOPOLYMERS 96 (4) 500 -500 2011年 [査読無し][通常論文]
  • Creation of a zinc finger type transcription factor responsive to Zn(II) concentration
    中屋智博, 今西未来, 森崎 達也, 能代 大輔, 二木史朗, 杉浦 幸雄 金属の関与する生体関連反応シンポジウム ,徳島 2010年06月25日 [査読無し][通常論文]
  • 亜鉛濃度に依存した新規転写調節系の開発
    中屋智博, 森崎 達也, 能代 大輔, 今西未来, 二木史朗, 杉浦 幸雄 日本ケミカルバイオロジー学会 第5回 年会 ,横浜 2010年05月18日 [査読無し][通常論文]
  • アラメチシンのアミノ酸置換とチャネル活性
    二木史朗, 野口晴加, 能代大輔, 浅見耕司 第46回ペプチド討論会 ,北九州 2009年11月05日 [査読無し][通常論文]
  • 金属イオンによる会合制御が可能なチャネル形成ペプチドの創製とその応用
    能代大輔, 浅見耕司, 二木史朗 第18回金属の関与する生体関連反応シンポジウム(SRM2008) ,名古屋 2008年06月05日 [査読無し][通常論文]
  • キレート形成原子団導入によるアラメチシンの会合安定化
    能代大輔, 浅見孝司, 二木史朗 第57回日本薬学会近畿支部大会 ,高槻 2007年10月27日 [査読無し][通常論文]
  • 金属によるチャンネル形成ペクチドの会合安定
    能代大輔, 浅見耕司, 二木史朗 第22回生体機能関連化学シンポジウム ,仙台 2007年09月28日 [査読無し][通常論文]
  • 金属イオンによるチャネル形成ペプチドの会合安定化 Metal-mediated stabilization of channel peptide assemblies
    能代大輔, 浅見孝司, 二木史朗 第22回生体機能関連化学シンポジウム ,仙台 2007年09月28日 [査読無し][通常論文]
  • 金属を認識する人工受容体型チャネルタンパク質の設計 Designing Artificial Metal-gated Ion Channels
    能代大輔, 園田和弘, 東野俊介, 浅見孝司, 二木史朗 日本ケミカルバイオロジー研究会 第2回年会 ,京都 2007年05月10日 [査読無し][通常論文]

共同研究・競争的資金等の研究課題

  • 液-液相分離によって生じるオートファゴソーム形成場の高速AFMによる観察
    日本学術振興会:若手研究
    研究期間 : 2019年04月 -2023年03月 
    代表者 : 能代 大輔
  • 高速AFMによる古細菌由来MCMタンパク質複合体の観察
    日本学術振興会:若手研究(B)
    研究期間 : 2017年04月 -2019年03月 
    代表者 : 能代大輔
  • センサー機能を有する人工イオンチャネルタンパク質の創製と展開
    日本学術振興会:特別研究員(DC1)
    研究期間 : 2009年04月 -2012年03月 
    代表者 : 能代大輔


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