2021/09/22 更新

写真b

ノザキ シンゴ
野崎 晋五
NOZAKI Shingo
*大学が定期的に情報更新している項目(その他は、researchmapの登録情報を転載)
所属*
理学部
職名*
助教
学位
博士(理学) ( 名古屋大学 )
学内職務経歴*
  • 2019年7月 - 現在 
    理学部   助教
 

研究分野

  • ライフサイエンス / 応用微生物学  / 合成生物学

論文

  • Exonuclease III (XthA) enforces in vivo DNA cloning of Escherichia coli to create cohesive ends 査読有り

    Nozaki S, Niki H

    Journal of Bacteriology201 ( 5 )   2019年2月

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  • The Ras1-Cdc42 pathway is involved in hyphal development of Schizosaccharomyces japonicus 査読有り

    Nozaki S, Furuya K, Niki H

    FEMS Yeast Research18 ( 4 )   2018年3月

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  • The Mechanism of Regulation of Pantothenate Biosynthesis by the PanD-PanZ·AcCoA Complex Reveals an Additional Mode of Action for the Antimetabolite N-Pentyl Pantothenamide (N5-Pan). 査読有り

    Arnott ZLP, Nozaki S, Monteiro DCF, Morgan HE, Pearson AR, Niki H, Webb ME

    Biochemistry56 ( 37 ) 4931 - 4939   2017年9月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    DOI: 10.1021/acs.biochem.7b00509

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  • The Structure of the PanD/PanZ Protein Complex Reveals Negative Feedback Regulation of Pantothenate Biosynthesis by Coenzyme A 査読有り

    Diana C. F. Monteiro, Vijay Patel, Christopher P. Bartlett, Shingo Nozaki, Thomas D. Grant, James A. Gowdy, Gary S. Thompson, Arnout P. Kalverda, Edward H. Snell, Hironori Niki, Arwen R. Pearson, Michael E. Webb

    CHEMISTRY & BIOLOGY22 ( 4 ) 492 - 503   2015年4月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:CELL PRESS  

    Coenzyme A (CoA) is an ubiquitous and essential cofactor, synthesized from the precursor pantothenate. Vitamin biosynthetic pathways are normally tightly regulated, including the pathway from pantothenate to CoA. However, no regulation of pantothenate biosynthesis has been identified. We have recently described an additional component in the pantothenate biosynthetic pathway, PanZ, which promotes the activation of the zymogen, PanD, to form aspartate a-decarboxylase (ADC) in a CoA-dependent manner. Here we report the structure of PanZ in complex with PanD, which reveals the structural basis for the CoA dependence of this interaction and activation. In addition, we show that PanZ acts as a CoA-dependent inhibitor of ADC catalysis. This inhibitory effect can effectively regulate the biosynthetic pathway to pantothenate, and thereby also regulate CoA biosynthesis. This represents a previously unobserved mode of metabolic regulation whereby a cofactor-utilizing protein negatively regulates the biosynthesis of the same cofactor.

    DOI: 10.1016/j.chembiol.2015.03.017

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  • Synchronous activation of cell division by light or temperature stimuli in the dimorphic yeast Schizosaccharomyces japonicus 査読有り

    Sho Okamoto, Kanji Furuya, Shingo Nozaki, Keita Aoki, Hironori Niki

    Eukaryotic Cell12 ( 9 ) 1235 - 1243   2013年9月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    Many fungi respond to light and regulate fungal development and behavior. A blue light-activated complex has been identified in Neurospora crassa as the product of the wc-1 and wc-2 genes. Orthologs of WC-1 and WC-2 have hitherto been found only in filamentous fungi and not in yeast, with the exception of the basidiomycete pathogenic yeast Cryptococcus. Here, we report that the fission yeast Schizosaccharomyces japonicus responds to blue light depending on Wcs1 and Wcs2, orthologs of components of the WC complex. Surprisingly, those of ascomycete S. japonicus are more closely related to those of the basidiomycete. S. japonicus reversibly changes from yeast to hyphae in response to environmental stresses. After incubation at 30°C, a colony of yeast was formed, and then hyphal cells extended from the periphery of the colony. When light cycles were applied, distinct dark- and bright-colored hyphal cell stripes were formed because the growing hyphal cells had synchronously activated cytokinesis. In addition, temperature cycles of 30°C for 12 h and 35°C for 12 h or of 25°C for 12 h and 30°C for 12 h during incubation in the dark induced a response in the hyphal cells similar to that of light. The stripe formation of the temperature cycles was independent of the wcs genes. Both light and temperature, which are daily external cues, have the same effect on growing hyphal cells. A dual sensing mechanism of external cues allows organisms to adapt to daily changes of environmental alteration. © 2013, American Society for Microbiology. All Rights Reserved.

    DOI: 10.1128/EC.00109-13

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  • Formation of a heterooctameric complex between aspartate alpha-decarboxylase and its cognate activating factor, PanZ, is CoA-dependent 査読有り

    Diana C. F. Monteiro, Michael D. Rugen, Dale Shepherd, Shingo Nozaki, Hironori Niki, Michael E. Webb

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS426 ( 3 ) 350 - 355   2012年9月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:ACADEMIC PRESS INC ELSEVIER SCIENCE  

    The existence of a fifth essential protein for pantothenate biosynthesis in some enteric bacteria has recently been reported by Stuecker et al. [10] and Nozaki et al. (in press) [9]. This protein, PanZ, catalyses the activation of the PanD zymogen to form ADC and is essential for prototrophic growth. In this paper, we characterise the interaction of PanZ with coenzyme A and a constitutively inactive mutant of PanD using a combination of isothermal titration calorimetry and mass spectrometry. These approaches reveal that the two proteins interact with nanomolar affinity in a CoA-dependent fashion to form a heterooctameric complex. (c) 2012 Elsevier Inc. All rights reserved.

    DOI: 10.1016/j.bbrc.2012.08.084

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  • An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli 査読有り

    Nozaki,S, Webb, M.E, Niki, H

    MicrobiologyOpen1 ( 3 ) 298 - 310   2012年9月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    国立遺伝学研究所以外の共著者あり

    DOI: 10.1002/mbo3.34

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  • Replication Initiator DnaA of Escherichia coli Changes Its Assembly Form on the Replication Origin during the Cell Cycle 査読有り

    Shingo Nozaki, Hironori Niki, Tohru Ogawa

    JOURNAL OF BACTERIOLOGY191 ( 15 ) 4807 - 4814   2009年8月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:AMER SOC MICROBIOLOGY  

    DnaA is a replication initiator protein that is conserved among bacteria. It plays a central role in the initiation of DNA replication. In order to monitor its behavior in living Escherichia coli cells, a nonessential portion of the protein was replaced by a fluorescent protein. Such a strain grew normally, and flow cytometry data suggested that the chimeric protein has no substantial loss of the initiator activity. The initiator was distributed all over the nucleoid. Furthermore, a majority of the cells exhibited certain distinct foci that emitted bright fluorescence. These foci colocalized with the replication origin (oriC) region and were brightest during the period spanning the initiation event. In cells that had undergone the initiation, the foci were enriched in less intense ones. In addition, a significant portion of the oriC regions at this cell cycle stage had no colocalized DnaA-enhanced yellow fluorescent protein (EYFP) focus point. It was difficult to distinguish the initiator titration locus (datA) from the oriC region. However, involvement of datA in the initiation control was suggested from the observation that, in Delta datA cells, DnaA-EYFP maximally colocalized with the oriC region earlier in the cell cycle than it did in wild-type cells and oriC concentration was increased.

    DOI: 10.1128/JB.00435-09

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  • Initiator titration complex formed at datA with the aid of IHF regulates replication timing in Escherichia coli 査読有り

    Shingo Nozaki, Yoshitaka Yamada, Tohru Ogawa

    GENES TO CELLS14 ( 3 ) 329 - 341   2009年3月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:WILEY-BLACKWELL PUBLISHING, INC  

    The initiation of replication in Escherichia coli is negatively controlled by a mechanism referred to as 'initiator titration', a process by which the initiator protein, DnaA, is titrated to newly replicated binding sequences on the chromosome to reduce the initiation potential for replication. Initiator titration occurs predominantly at the datA locus that binds exceptionally large amounts of DnaA molecules to prevent aberrant initiations. We found that this was enabled by integration host factor (IHF). Within datA, there is a consensus IHF recognition sequence between the two DnaA recognition sequences (DnaA boxes) essential for its function. Binding of IHF to this site was demonstrated both in vitro and in vivo. Disruption of the core sequence in the consensus of the IHF-binding resulted in increased origin concentration as observed in Delta datA cells. Furthermore, the number of DnaA molecules bound to datA was reduced in cells carrying a disruption in the IHF-binding core sequence. The IHF-binding site and the essential DnaA boxes had to be located at a proper distance and orientation to maintain the accurate initiation timing. Therefore, IHF is a unique element in the control of replication initiation that acts negatively at datA, while known to act as a positive regulator at oriC.

    DOI: 10.1111/j.1365-2443.2008.01269.x

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  • Determination of the minimum domain II size of Escherichia coli DnaA protein essential for cell viability 査読有り

    Shingo Nozaki, Tohru Ogawa

    MICROBIOLOGY-SGM154 ( 11 ) 3379 - 3384   2008年11月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:SOC GENERAL MICROBIOLOGY  

    The DnaA protein is the bacterial initiator of replication at a unique chromosomal site, oriC. It is present in all bacterial species and has a conserved structure with four domains. The structures of domains I and III-IV have been solved recently for some bacterial species, and the molecular process leading to the initiation event has been investigated in detail. On the other hand, domain II appears to have no rigid structure and is assumed to be a flexible linker connecting the N-terminal domain I and the C-terminal domains III-IV. It differs significantly in length and amino acid sequence among bacterial species. Whether or not domain II has any function(s) to initiate replication is unknown. The precise borders at both of its ends as well as its essential portions for cell viability are also unknown. In this study, we introduced systematic deletions into the domain II region on the chromosomal dnaA gene of Escherichia coli and examined their effect on cell physiology. Stretches of 30-36 consecutive amino acid residues could be deleted from various portions between the 78th and the 136th residues without affecting cell viability. We propose that domain II of E coli DnaA is from the 79th to the 135th residues and at least 21-27 residues are required as a spacer to keep domains I and III-IV in the correct positions.

    DOI: 10.1099/mic.0.2008/019745-0

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講演・口頭発表等

  • バクテリオファージを活用した長鎖DNAアセンブリー

    野崎晋五

    第17回21世紀大腸菌研究会  2021年8月20日 

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  • 大腸菌ゲノムより見出された形質転換に関与する遺伝子群

    野崎晋五, 仁木宏典

    第14回日本ゲノム微生物学会年会  2020年3月7日 

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  • 大腸菌細胞内でのDNAクローニング(iVEC)のメカニズムとその応用

    野崎晋五, 仁木宏典

    第1回日本遺伝学会春季分科会  2019年3月8日 

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  • 簡便な大腸菌形質転換法を用いたDNA取り込みに関与する遺伝子群のスクリーニング

    野崎晋五, 仁木宏典

    第15回21世紀大腸菌研究会  2018年5月25日 

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  • 大腸菌におけるDNA取り込みに関与する遺伝子群の網羅的探索

    野崎晋五, 仁木宏典

    第12回日本ゲノム微生物学会年会  2018年3月6日 

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  • NBRPバイオリソースiVEC: 大腸菌細胞内でのDNAクローニングのメカニズムとさらなる高機能化

    野崎晋五, 仁木宏典

    第24回複製・組換え・修復ワークショップ  2017年11月28日 

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  • iVEC: 大腸菌細胞内でのDNAクローニングとそのメカニズム

    野崎晋五, 仁木宏典

    第14回21世紀大腸菌研究会  2017年6月9日 

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  • iVEC: 大腸菌細胞内でのDNAクローニング方法

    野崎晋五, 仁木宏典

    第39回日本分子生物学会年会  2016年11月30日 

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    記述言語:日本語  

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  • iVEC: a simple cloning method by using in vivo recombination of E. coli 国際会議

    Nozaki, S, Niki, H

    The 10th 3R Symposium  2016年11月14日 

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    記述言語:英語  

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  • National BioResource Project (NBRP) E. coli and B. subtilis 国際会議

    Nozaki S, Niki H

    The 8th ANRRC International Meeting  2016年9月21日 

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    記述言語:英語  

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  • Ras-Cdc42経路はジャポニカス分裂酵母の菌糸形成と接合の両方に関与する

    野崎晋五, 古谷寛治, 仁木宏典

    第48回酵母遺伝学フォーラム研究報告会  2015年9月2日 

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    記述言語:日本語  

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  • Crostalk between the mating and hyphal transition at early steps of the Ras-MAPK signal transduction pathway in Schizosaccharomyces japonicus 国際会議

    Nozaki S, Furuya, K, Niki H

    8th International Fission Yeast Meeting  2015年6月21日 

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    記述言語:英語  

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  • Schizosaccharomyces japonicusの菌糸転換におけるCdc2の役割

    野崎晋五, 仁木宏典

    第37回日本分子生物学会年会  2014年11月26日 

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    会議種別:ポスター発表  

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  • Involvement of the inhibition of Cdc2 activity during the yeast cell cycle in hyphal development of Schizosaccharomyces japonicus 国際会議

    Nozaki, S, Furuya, K, Niki, H

    The 9th 3R symposium  2014年11月18日 

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    会議種別:ポスター発表  

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  • ジャポニカス分裂酵母の菌糸形成に関与する遺伝子の探索

    野崎晋五, 古谷寛治, 吉川博文, 仁木宏典

    第47回酵母遺伝学フォーラム研究報告会  2014年9月1日 

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    会議種別:ポスター発表  

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  • ジャポニカス分裂酵母ゲノムより得られた菌糸形成に関与する遺伝子群

    野崎晋五, 古谷寛治, 吉川博文, 仁木宏典

    第8回日本ゲノム微生物学会年会  2014年3月7日 

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    会議種別:ポスター発表  

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  • Genetic analysis of mutants that are defective in hyphal development of Schizosaccharomyces japonicus 国際会議

    Nozaki, S, Furuya, K, Niki, H

    7th International Fission Yeast Meeting  2013年6月24日 

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    会議種別:ポスター発表  

    開催地:London  

    国立遺伝学研究所以外との共同発表あり

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  • 新奇因子PanZによる大腸菌におけるパントテン酸・CoA合成の制御機構

    野崎晋五, 仁木宏典

    第35回日本分子生物学会年会  2012年12月11日 

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    会議種別:ポスター発表  

    開催地:福岡  

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  • 新規因子PanZによるアスパラギン酸-α-脱炭酸酵素の活性制御

    野崎晋五, 仁木宏典

    第9回 21世紀大腸菌研究会  2012年6月21日 

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    会議種別:口頭発表(一般)  

    開催地:長浜  

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  • γプロテオバクテリアに現れたパントテン酸合成の新規制御因子PanZ

    野崎晋五, 仁木宏典

    第6回日本ゲノム微生物学会年会  2012年3月11日 

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    会議種別:ポスター発表  

    開催地:池袋  

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  • 新規因子PanZによるピルボイル酵素PanDの活性制御

    野崎晋五, 仁木宏典

    第8回 21世紀大腸菌研究会  2011年5月18日 

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    会議種別:口頭発表(一般)  

    開催地:南木曽  

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  • Regulation of DnaA assembly at oriC in Escherichia coli 国際会議

    Nozaki, S, Niki, H, Ogawa, T

    The 6th 3R symposium  2010年10月27日 

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    会議種別:ポスター発表  

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  • DnaAタンパク質の細胞内局在変化による染色体複製の開始制御

    野崎晋五, 仁木宏典, 小川徹

    第7回21世紀大腸菌研究会  2010年6月3日 

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    会議種別:口頭発表(一般)  

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  • Subcellular localization of Escherichia coli DnaA protein

    Nozaki, S, Niki, H, Ogawa, T

    EMBO Workshop “Frontiers of prokaryotic cell biology”  2009年8月 

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  • Subcellular localization of Escherichia coli DnaA, the initiator of DNA replication

    Nozaki, S, Niki, H, Ogawa, T

    Keystone symposia “DNA replication and recombination”  2008年2月 

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共同研究・競争的資金等の研究

  • ボトルシップ法による人工細菌の創出

    JST戦略的創造研究推進事業  さきがけ 

    野崎晋五

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    2019年10月 - 2023年3月

    担当区分:研究代表者 

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  • 大腸菌の形質転換におけるDNA取り込みメカニズムの解明

    日本学術振興会  科学研究費助成事業 基盤研究(C) 

    野崎 晋五

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    2019年4月 - 2022年3月

    課題番号:19K05782

    配分額:4420000円 ( 直接経費:3400000円 、 間接経費:1020000円 )

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