Study of corrosion and degradation of the objects in the nuclear reactor by microorganisms (Contract research); FY2020 Nuclear Energy Science & Technology and Human Resource Development Project

Collaborative Laboratories for Advanced Decommissioning Science; Keio University*

JAEA-Review 2021-048, 181 Pages, 2022/01

JAEA-Review-2021-048.pdf:14.5MB

The Collaborative Laboratories for Advanced Decommissioning Science (CLADS), Japan Atomic Energy Agency (JAEA), had been conducting the Nuclear Energy Science & Technology and Human Resource Development Project (hereafter referred to "the Project") in FY2020. The Project aims to contribute to solving problems in the nuclear energy field represented by the decommissioning of the Fukushima Daiichi Nuclear Power Station (1F), Tokyo Electric Power Company Holdings, Inc. (TEPCO). For this purpose, intelligence was collected from all over the world, and basic research and human resource development were promoted by closely integrating/collaborating knowledge and experiences in various fields beyond the barrier of conventional organizations and research fields. The sponsor of the Project was moved from the Ministry of Education, Culture, Sports, Science and Technology to JAEA since the newly adopted proposals in FY2018. On this occasion, JAEA constructed a new research system where JAEA-academia collaboration is reinforced and medium-to-long term research/development and human resource development contributing to the decommissioning are stably and consecutively implemented. Among the adopted proposals in FY2019, this report summarizes the research results of the "Study of corrosion and degradation of the objects in the nuclear reactor by microorganisms" conducted in FY2019 and FY2020. Since the final year of this proposal was FY2020, the results for two fiscal years were summarized. The purpose of the study is to obtain knowledge related to microorganisms that will be useful in the decommissioning process of 1F. Therefore, we clarified the current conditions of the microbial community inhabiting the power plant and its premises. Environmental samples were taken from several sites such as, topsoil from the south of the plant site boundary (south of the treated water tanks), seabed soil and its above water near the plant, surface water 3km offshore …

Editorial: Maintenance of genome integrity; DNA damage sensing, signaling, repair, and replication in plants

Balestrazzi, A.*; Achary V Mohan Murali*; Macovei, A.*; Yoshiyama, Kaoru*; Sakamoto, Ayako

Frontiers in Plant Science (Internet), 7, p.64_1 - 64_2, 2016/02

https://doi.org/10.3389/fpls.2016.00064

no abstracts in English

Draft genome sequence of sp. ME121, isolated from soil as a mixed single colony with sp. 32K

Fujinami, Shun*; Takeda, Kiyoko*; Onodera, Takefumi*; Sato, Katsuya; Shimizu, Tetsu*; Wakabayashi, Yu*; Narumi, Issey*; Nakamura, Akira*; Ito, Masahiro*

Genome Announcements (Internet), 3(5), p.e01005-15_1 - e01005-15_2, 2015/09

https://doi.org/10.1128/genomeA.01005-15

Draft genome sequence of calcium-dependent sp. strain TCA20, isolated from a hot spring containing a high concentration of calcium ions

Fujinami, Shun*; Takeda, Kiyoko*; Onodera, Takefumi*; Sato, Katsuya; Sano, Motohiko*; Takahashi, Yuka*; Narumi, Issey*; Ito, Masahiro*

Genome Announcements (Internet), 2(5), p.e00866-14_1 - e00866-14_2, 2014/09

https://doi.org/10.1128/genomeA.00866-14

Enlarged FAMSBAS; Protein 3D structure models of genome sequences for 41 species

Yamaguchi, Akihiro*; Iwadate, Mitsuo*; Suzuki, Eiichiro*; Yura, Kei; Kawakita, Shigetsune*; Umeyama, Hideaki*; Go, Michiko*

Nucleic Acids Research, 31(1), p.463 - 468, 2003/01

https://doi.org/10.1093/nar/gkg117

Enlarged FAMSBASE is a relational database of comparative protein structure models for the whole genome of 41 species, presented in the GTOP database. The models are calculated by FAMS, Full Automatic Modeling System. Enlarged FAMSBASE provides a wide range of query keys, such as name of ORF (open reading frame), ORF keywords, PDB ID, PDB heterogen atoms, and sequence similarity. Heterogen atoms in PDB include cofactors, ligands, and other factors that interact with proteins, and are a good starting point for analyzing interactions between proteins and other molecules. The data may also work as a template for drug design. The present number of ORFs with protein 3D models in FAMSBASE is 183,805, and the database includes an average of three models for each ORF. FAMSBASE is available at http://famsbase.bio.nagoya-u.ac.jp/famsbase/.