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Novel mechanisms for the removal of strong replication-blocking HMCES- and thiazolidine-DNA adducts in humans 査読有り国際誌

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

NUCLEIC ACIDS RESEARCH 51 巻 ( 10 ) 頁： 4959 - 4981 2023年6月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Nucleic Acids Research

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 ?-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

RFWD3 and translesion DNA polymerases contribute to PCNA modification-dependent DNA damage tolerance 査読有り国際誌

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

LIFE SCIENCE ALLIANCE 5 巻 ( 12 ) 頁： e202201584 2022年12月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Life Science Alliance

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

哺乳類細胞における紫外線損傷の損傷乗り越えDNA合成とその制御招待有り査読有り

金尾　梨絵

放射線生物研究 55 巻 ( 1 ) 頁： 25-42 2020年3月

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 294 巻 ( 11 ) 頁： 4177 - 4187 2019年3月

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年10月

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 803 巻頁： 82 - 88 2017年10月

USP7 Is a Suppressor of PCNA Ubiquitination and Oxidative Stress-Induced Mutagenesis in Human Cells 査読有り

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

Cell Reports 13 巻頁： 2072-2080 2015年12月

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

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

Nucleic Acids Res. 43 巻 ( 16 ) 頁： 7898-7910 2015年9月

UV-induced mutagenesis in epidermal cells of mice defective in DNA polymerase η and/or ι 査読有り

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

DNA Repair (Amst.) 29 巻頁： 139-146 2015年5月

Relevance of Simultaneous Mono-Ubiquitinations of Multiple Units of PCNA Homo-Trimers in DNA Damage Tolerance. 査読有り

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

PLoS One 10 巻頁： e0118775 2015年2月

Guanine- 5-carboxylcytosine base pairs mimic mismatches during DNA replication. 査読有り

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. 4 巻 2014年

A novel interaction between human DNA polymerase η and MutLα 査読有り

Rie Kanao, Fumio Hanaoka, and Chikahide Masutani

Biochemical and Biophysical Research Communications 389 巻頁： 40-45 2009年

UV-B radiation induces epithelial tumors in mice lacking DNA polymerase η and mesenchymal tumors in mice deficient for DNA polymerase ι 査読有り

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 26 巻 ( 20 ) 頁： 7696-7706 2006年

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