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dc.contributor.author | Yokogawa, Mariko | en |
dc.contributor.author | Tsushima, Takashi | en |
dc.contributor.author | Noda, Nobuo N. | en |
dc.contributor.author | Kumeta, Hiroyuki | en |
dc.contributor.author | Enokizono, Yoshiaki | en |
dc.contributor.author | Yamashita, Kazuo | en |
dc.contributor.author | Standley, Daron M. | en |
dc.contributor.author | Takeuchi, Osamu | en |
dc.contributor.author | Akira, Shizuo | en |
dc.contributor.author | Inagaki, Fuyuhiko | en |
dc.contributor.alternative | 竹内, 理 | ja |
dc.contributor.transcription | タケウチ, オサム | ja |
dc.date.accessioned | 2016-07-14T05:07:57Z | - |
dc.date.available | 2016-07-14T05:07:57Z | - |
dc.date.issued | 2016-03-01 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | http://hdl.handle.net/2433/216019 | - |
dc.description.abstract | Regnase-1 is an RNase that directly cleaves mRNAs of inflammatory genes such as IL-6 and IL-12p40, and negatively regulates cellular inflammatory responses. Here, we report the structures of four domains of Regnase-1 from Mus musculus - the N-terminal domain (NTD), PilT N-terminus like (PIN) domain, zinc finger (ZF) domain and C-terminal domain (CTD). The PIN domain harbors the RNase catalytic center; however, it is insufficient for enzymatic activity. We found that the NTD associates with the PIN domain and significantly enhances its RNase activity. The PIN domain forms a head-to-tail oligomer and the dimer interface overlaps with the NTD binding site. Interestingly, mutations blocking PIN oligomerization had no RNase activity, indicating that both oligomerization and NTD binding are crucial for RNase activity in vitro. These results suggest that Regnase-1 RNase activity is tightly controlled by both intramolecular (NTD-PIN) and intermolecular (PIN-PIN) interactions. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Nature Publishing Group | en |
dc.rights | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ | en |
dc.title | Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.jtitle | Scientific Reports | en |
dc.identifier.volume | 6 | - |
dc.relation.doi | 10.1038/srep22324 | - |
dc.textversion | publisher | - |
dc.identifier.artnum | 22324 | - |
dc.identifier.pmid | 26927947 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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