MASUI Ryoji

写真a

Search Institutional Repository


Title

Professor

Laboratory location

Sugimoto Campus

Mail Address

E-mail address

Degree 【 display / non-display

  • Osaka University -  Ph.D

Research Areas 【 display / non-display

Structural biochemistry

Awards & Honors 【 display / non-display

  • The 11th Symposium of Protein Society (Boston, U.S.A.) Award for Best Posters

    1997  

Current Career 【 display / non-display

  • Osaka City University   Graduate School of Science   Biology and Geosciences Course   Professor  

Graduating School 【 display / non-display

  • 1983.04
    -
    1988.03

    Osaka University   Faculty of Science  

 

Published Papers 【 display / non-display

  • Resistance to UV irradiation caused by inactivation of nurA and herA genes in Thermus thermophilus

    Fujii, Y., Inoue, M., Fukui, K., Kuramitsu, S., Masui, R.

    Journal of Bacteriology  200 ( 16 ) e00201-18 2018.07  [Refereed]

     View Summary

    NurA and HerA are thought to be essential proteins for DNA end resection in archaeal homologous recombination systems. Thermus thermophilus, an extremely thermophilic eubacterium, has proteins that exhibit significant sequence similarity to archaeal NurA and HerA. To unveil the cellular function of NurA and HerA in T. thermophilus, we performed phenotypic analysis of disruptant mutants of nurA and herA with or without DNA-damaging agents. The nurA and herA genes were not essential for survival, and their deletion had no effect on cell growth and genome integrity. Unexpectedly, these disruptants of T. thermophilus showed increased resistance to UV irradiation and mitomycin C treatment. Further, these disruptants and the wild type displayed no difference in sensitivity to oxidative stress and a DNA replication inhibitor. T. thermophilus NurA had nuclease activity, and HerA had ATPase. The overexpression of loss-of-function mutants of nurA and herA in the respective disruptants showed no complementation, suggesting their enzymatic activities were involved in the UV sensitivity. In addition, T. thermophilus NurA and HerA interacted with each other in vitro and in vivo, forming a complex with 2:6 stoichiometry. These results suggest that the NurA-HerA complex has an architecture similar to that of archaeal counterparts but that it impairs, rather than promotes, the repair of photoproducts and DNA cross-links in T. thermophilus cells. This cellular function is distinctly different from that of archaeal NurA and HerA.

    DOI PubMed

  • Indispensable residue for uridine binding in the uridine-cytidine kinase family

    Tomoike, F., Nakagawa, N., Fukui, K., Yano, T., Kuramitsu, S., Masui, R.

    Biochemistry and Biophysics Reports1  11   93 - 98 2017.07  [Refereed]

  • The Lon protease-like domain in the bacterial RecA paralog RadA is required for DNA binding and repair

    Inoue Masao, Fukui Kenji, Fujii Yuki, Nakagawa Noriko, Yano Takato, Kuramitsu Seiki, Masui Ryoji

    Journal of Biological Chemistry  292 ( 23 ) 9801 - 9814 2017.06  [Refereed]

     View Summary

    Homologous recombination (HR) plays an essential role in the maintenance of genome integrity. RecA/Rad51 paralogs have been recognized as an important factor of HR. Among them, only one bacterial RecA/Rad51 paralog, RadA, is involved in HR as an accessory factor of RecA recombinase. RadA has a unique Lon protease-like domain (LonC) at its C terminus, in addition to a RecA-like ATPase domain. Unlike Lon protease, RadA's LonC domain does not show protease activity but is still essential for RadA-mediated DNA repair. Reconciling these two facts has been difficult because RadA's tertiary structure and molecular function are unknown. Here, we describe the hexameric ring structure of RadA's LonC domain, as determined by X-ray crystallography. The structure revealed the two positively charged regions unique to the LonC domain of RadA are located at the intersubunit cleft and the central hole of a hexameric ring. Surprisingly, a functional domain analysis demonstrated the LonC domain of RadA binds DNA, with site-directed mutagenesis showing that the two positively charged regions are critical for this DNA-binding activity. Interestingly, only the intersubunit cleft was required for the DNA-dependent stimulation of ATPase activity of RadA, and at least the central hole was essential for DNA repair function. Our data provide the structural and functional features of the LonC domain and their function in RadA-mediated DNA repair.

    DOI PubMed

  • Proteome-wide identification of lysine propionylation in thermophilic and mesophilic bacteria: Geobacillus kaustophilus, Thermus thermophilus, Escherichia coli, Bacillus subtilis, and Rhodothermus marinus

    Okanishi Hiroki, Kim Kwang, Masui Ryoji, Kuramitsu Seiki

    Extremophiles  21 ( 2 ) 283 - 296 2017.03  [Refereed]

    DOI

  • Proteome-wide identification of lysine succinylation in thermophilic and mesophilic bacteria

    Okanishi Hiroki, Kim Kwang, Fukui Kenji, Yano Takato, Kuramitsu Seiki, Masui Ryoji

    Biochimica et Biophysica Acta  1865 ( 2 ) 232 - 242 2017.02  [Refereed]

    DOI

display all >>

Books etc 【 display / non-display

  • Enzymic reaction of proteins

    (Part: Single Work )

    2009.08

  • Atomic biology in post-genome era

    (Part: Joint Work )

    2004.08

Review Papers (Misc) 【 display / non-display

  • Acyl-Proteome with Protein Tertiary Structure Information Reveals the Significance of Lysine Acylations

    Okanishi Hiroki, Masui Ryoji, Kim Kwang, Kuramitsu Seiki

    Japanese Proteome Society Proteome Letters  3 ( 1 ) 15 - 22 2018.07  [Refereed]  [Invited]

  • Structural Analysis of a Protease-like Protein with DNA-binding Activity

    The Crystallographic Society of Japan, Journal of the Crystallographic Society of Japan  60 ( 2 ) 74 - 75 2018  [Refereed]  [Invited]

  • Functional analysis of new proteases from an extremely thermophilic organism, Thermus theromphilus HB8

    Yumi Kimura, Daisuke Sasaki, Naoya Fujimura, Tadashi Ono, Chinami Sako, Suzuka Yamasaki, Ryoji Masui, Noriko Nakagawa

    Protein Science  26   92 - 92 2017

  • Discovery of Lys propionylation as one of abundant post-translational modifications

    Okanishi Hiroki, Kim Kwang, Nakagawa Noriko, Kuramitsu Seiki, Masui Ryouji

    Japanese Proteome Society Proteome Letters  2015   183 - 183 2015

  • Molecular mechanisms of the whole DNA repair system: A comparison of bacterial and eukaryotic systems

    Morita, R., Nakane, S., Shimada, A., Inoue, M., Iino, H., Wakamatsu, T., Fukui, K., Nakagawa, N., Masui, R., Kuramitsu, S.

    Journal of Nucleic Acids  2010   179594 2010.10  [Refereed]  [Invited]

display all >>

Conference Activities & Talks 【 display / non-display

  • CMPキナーゼによる基質認識の構造的基盤

    妻鹿良亮,中川紀子,倉光成紀,増井良治

    第42回 日本分子生物学会年会  2019.12 

  • Structural and functional domain analysis of fatty acid kinase

    Maya Nakatani, Taihei Murakami, Hiroki Okanishi, Makoto Miyata, Ryoji Masui

    The 42nd Annual Meeting of the Moleular Bioloy Society of Japan  2019.12 

  • NurA and HerA in bacteria contribute to the repair of UV-induced lesions with recombination mediator proteins

    Yuki Fujii, Masao Inoue, Kenji Fukui, Ryoji Masui

    The 42nd Annual Meeting of the Moleular Bioloy Society of Japan  2019.12 

  • Mechanism of drastic stabilization by ATP of a thermophilic protein kinase structure

    Yusuke Fujino, Masao Inoue, Yuki Fujii, Ryoji Masui

    The 20th Annual Meeting of the Japanese Society for Extremophiles  2019.11 

  • Structural basis for ligand binding to CMP kinase revealed by X-ray crystallographic analysis of the different liganded forms

    Ryosuke Mega, Noriko Nakagawa, Seiki Kuramitsu, Ryoji Masui

    The 92nd Annual Meeting of the Japanese Biochemical Society  2019.09 

display all >>

 

Other educational activity and Special note 【 display / non-display

  • Improvement of educational methods

    (2019)

  • Contribution to FD activities

    (2019)

  • Class teacher

    (2019)

  • Contribution to FD activities

    (2018)

  • Class teacher

    (2018)

display all >>