Updated on 2023/09/08

写真a

 
KANAO, Rie
 
Organization
Research Institute of Environmental Medicine Division of Stress Adaptation and Protection Assistant Professor
Graduate School
Graduate School of Medicine
Title
Assistant Professor
Contact information
メールアドレス
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Degree 1

  1. 博士(薬学) ( 2009.3   大阪大学 ) 

Research Interests 2

  1. translesion synthesis

  2. DNA damage tolerance

Research History 3

  1. 名古屋大学 環境医学研究所 助教

    2010.11

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    Country:Japan

  2. 名古屋大学 環境医学研究所 研究員

    2010.9 - 2010.10

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    Country:Japan

  3. 大阪大学大学院生命機能研究科 特任研究員

    2009.4 - 2010.8

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    Country:Japan

Education 3

  1. Osaka University   Graduate School, Division of Pharmaceutical Sciences

    2006.4 - 2009.3

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    Country: Japan

  2. Osaka University   Graduate School, Division of Pharmaceutical Sciences

    2004.4 - 2006.3

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    Country: Japan

  3. Osaka University   Faculty of Pharmaceutical Science

    2000.4 - 2004.3

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    Country: Japan

Professional Memberships 4

  1. 日本分子生物学会

  2. 日本癌学会

  3. 日本薬学会

  4. 日本放射線影響学会

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Papers 13

  1. Novel mechanisms for the removal of strong replication-blocking HMCES- and thiazolidine-DNA adducts in humans. Reviewed International journal

    Yohei Sugimoto, Yuji Masuda, Shigenori Iwai, Yumi Miyake, Rie Kanao, Chikahide Masutani

    Nucleic acids research   Vol. 51 ( 10 ) page: 4959 - 4981   2023.6

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    Language:English   Publishing type:Research paper (scientific journal)  

    Apurinic/apyrimidinic (AP) sites are DNA lesions created under normal growth conditions that result in cytotoxicity, replication-blocks, and mutations. AP sites are susceptible to β-elimination and are liable to be converted to DNA strand breaks. HMCES (5-hydroxymethylcytosine binding, ES cell specific) protein interacts with AP sites in single stranded (ss) DNA exposed at DNA replication forks to generate a stable thiazolidine protein-DNA crosslink and protect cells against AP site toxicity. The crosslinked HMCES is resolved by proteasome-mediated degradation; however, it is unclear how HMCES-crosslinked ssDNA and the resulting proteasome-degraded HMCES adducts are processed and repaired. Here, we describe methods for the preparation of thiazolidine adduct-containing oligonucleotides and determination of their structure. We demonstrate that the HMCES-crosslink is a strong replication blocking adduct and that protease-digested HMCES adducts block DNA replication to a similar extent as AP sites. Moreover, we show that the human AP endonuclease APE1 incises DNA 5' to the protease-digested HMCES adduct. Interestingly, while HMCES-ssDNA crosslinks are stable, the crosslink is reversed upon the formation of dsDNA, possibly due to a catalytic reverse reaction. Our results shed new light on damage tolerance and repair pathways for HMCES-DNA crosslinks in human cells.

    DOI: 10.1093/nar/gkad246

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  2. RFWD3 and translesion DNA polymerases contribute to PCNA modification-dependent DNA damage tolerance. Reviewed International journal

    Rie Kanao, Hidehiko Kawai, Toshiyasu Taniguchi, Minoru Takata, Chikahide Masutani

    Life science alliance   Vol. 5 ( 12 ) page: e202201584   2022.12

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    Language:English   Publishing type:Research paper (scientific journal)  

    DNA damage tolerance pathways are regulated by proliferating cell nuclear antigen (PCNA) modifications at lysine 164. Translesion DNA synthesis by DNA polymerase η (Polη) is well studied, but less is known about Polη-independent mechanisms. Illudin S and its derivatives induce alkyl DNA adducts, which are repaired by transcription-coupled nucleotide excision repair (TC-NER). We demonstrate that in addition to TC-NER, PCNA modification at K164 plays an essential role in cellular resistance to these compounds by overcoming replication blockages, with no requirement for Polη. Polκ and RING finger and WD repeat domain 3 (RFWD3) contribute to tolerance, and are both dependent on PCNA modifications. Although RFWD3 is a FANC protein, we demonstrate that it plays a role in DNA damage tolerance independent of the FANC pathway. Finally, we demonstrate that RFWD3-mediated cellular survival after UV irradiation is dependent on PCNA modifications but is independent of Polη. Thus, RFWD3 contributes to PCNA modification-dependent DNA damage tolerance in addition to translesion DNA polymerases.

    DOI: 10.26508/lsa.202201584

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  3. Translesion synthesis for UV-induced DNA lesions in mammalian cells Invited Reviewed

    Rie Kanao

    Radiation Biology Research Communications   Vol. 55 ( 1 ) page: 25-42   2020.3

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    Authorship:Lead author   Language:Japanese  

  4. Preferential digestion of PCNA-ubiquitin and p53-ubiquitin linkages by USP7 to remove polyubiquitin chains from substrates

    Masuda Yuji, Kanao Rie, Kawai Hidehiko, Kukimoto Iwao, Masutani Chikahide

    JOURNAL OF BIOLOGICAL CHEMISTRY   Vol. 294 ( 11 ) page: 4177 - 4187   2019.3

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1074/jbc.RA118.005167

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  5. Regulation of HLTF-mediated PCNA polyubiquitination by RFC and PCNA monoubiquitination levels determines choice of damage tolerance pathway.

    Masuda Y, Mitsuyuki S, Kanao R, Hishiki A, Hashimoto H, Masutani C

    Nucleic acids research     2018.10

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/nar/gky943

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  6. Regulation of DNA damage tolerance in mammalian cells by post-translational modifications of PCNA

    Kanao Rie, Masutani Chikahide

    MUTATION RESEARCH-FUNDAMENTAL AND MOLECULAR MECHANISMS OF MUTAGENESIS   Vol. 803   page: 82 - 88   2017.10

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1016/j.mrfmmm.2017.06.004

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  7. USP7 Is a Suppressor of PCNA Ubiquitination and Oxidative Stress-Induced Mutagenesis in Human Cells Reviewed

    Kashiwaba S, Kanao R, Masuda Y, Kusumoto-Matsuo R, Hanaoka F, Masutani C

    Cell Reports   Vol. 13   page: 2072-2080   2015.12

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    Authorship:Lead author   Language:English   Publishing type:Research paper (scientific journal)  

  8. Different types of interaction between PCNA and PIP boxes contribute to distinct cellular functions of Y-family DNA polymerases. Reviewed

    Masuda Y, Kanao R, Kaji K, Ohmori H, Hanaoka F, Masudani C

    Nucleic Acids Res.   Vol. 43 ( 16 ) page: 7898-7910   2015.9

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/nar/gkv712

  9. UV-induced mutagenesis in epidermal cells of mice defective in DNA polymerase η and/or ι Reviewed

    Kanao R., Yokoi M., Ohkumo T., Sakurai Y., Dotsu K., Kura S., Nakatsu Y., Tsuzuki T., Masutani C., Hanaoka F.

    DNA Repair (Amst.)   Vol. 29   page: 139-146   2015.5

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    DOI: 10.1016/j.dnarep.2015.02.006.

  10. Relevance of Simultaneous Mono-Ubiquitinations of Multiple Units of PCNA Homo-Trimers in DNA Damage Tolerance. Reviewed

    Kanao R., Masuda Y., Deguchi S., Yumoto-Sugimoto M., Hanaoka F., Masutani C

    PLoS One   Vol. 10   page: e0118775   2015.2

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    Authorship:Lead author   Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1371/journal.pone.0118775

  11. Guanine- 5-carboxylcytosine base pairs mimic mismatches during DNA replication. Reviewed

    Shibutani, T., Ito, S., Toda, M., Kanao, R., Collins, L.B., Shibata, M., Urabe, M., Koseki, H., Masuda, Y., Swenberg, J.A., Masutani, C., Hanaoka, F., Iwai, S., Kuraoka, I.

    Sci. Rep.   Vol. 4   2014

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1038/srep05220

  12. A novel interaction between human DNA polymerase η and MutLα Reviewed

    Rie Kanao, Fumio Hanaoka, and Chikahide Masutani

    Biochemical and Biophysical Research Communications   Vol. 389   page: 40-45   2009

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    Authorship:Lead author   Language:English   Publishing type:Research paper (scientific journal)  

  13. UV-B radiation induces epithelial tumors in mice lacking DNA polymerase η and mesenchymal tumors in mice deficient for DNA polymerase ι Reviewed

    Tsuyoshi Ohkumo, Yuji Kondo, Masayuki Yokoi, Testuya Tsukamoto, Ayumi Yamada, Taiki Sugimoto, Rie Kanao, Yujiro Higashi, Hisato Kondoh, Masae Tatematsu, Chikahide Masutani, and Fumio Hanaoka

    Molecular and Cellular Biology   Vol. 26 ( 20 ) page: 7696-7706   2006

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    Language:English   Publishing type:Research paper (scientific journal)  

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KAKENHI (Grants-in-Aid for Scientific Research) 1

  1. PCNAのユビキチン化で制御される新規DNA損傷トレランス経路の解析

    Grant number:21K12238  2021.4 - 2024.3

    科学研究費助成事業  基盤研究(C)

    金尾 梨絵

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    Authorship:Principal investigator 

    Grant amount:\4030000 ( Direct Cost: \3100000 、 Indirect Cost:\930000 )

    細胞が増殖するためには細胞分裂に先立ち、ゲノムDNAをコピーするDNA複製が必要であるが、放射線、紫外線、化学物質などにより生じたDNA上の損傷はDNA複製の妨げとなる。細胞にはDNA損傷が生じても複製を継続するためのDNA損傷トレランスと呼ばれるメカニズムが備わっているが、ヒト細胞において、その全容はまだ明らかになっていない。本研究はヒト細胞のDNA損傷トレランスのメカニズムを明らかにしようとするものである。