フルテキストURL Nature_556_209.pdf
著者 Yu, Long-Jiang| Suga, Michihiro| Wang-Otomo, Zheng-Yu| Shen, Jian-Ren|
抄録 Light-harvesting complex 1 (LH1) and the reaction centre (RC) form a membrane-protein supercomplex that performs the primary reactions of photosynthesis in purple photosynthetic bacteria. The structure of the LH1-RC complex can provide information on the arrangement of protein subunits and cofactors; however, so far it has been resolved only at a relatively low resolution. Here we report the crystal structure of the calcium-ion-bound LH1-RC supercomplex of Thermochromatium tepidum at a resolution of 1.9 Å. This atomic-resolution structure revealed several new features about the organization of protein subunits and cofactors. We describe the loop regions of RC in their intact states, the interaction of these loop regions with the LH1 subunits, the exchange route for the bound quinone QB with free quinone molecules, the transport of free quinones between the inside and outside of the LH1 ring structure, and the detailed calcium-ion-binding environment. This structure provides a solid basis for the detailed examination of the light reactions that occur during bacterial photosynthesis.
備考 This is an Accepted Manuscript of an article published by Springer Nature
発行日 2018-04-04
出版物タイトル Nature
556巻
出版者 Springer Nature
開始ページ 209
終了ページ 213
ISSN 0028-0836
NCID AA00752384
資料タイプ 学術雑誌論文
言語 English
OAI-PMH Set 岡山大学
論文のバージョン author
PubMed ID 29618814
DOI 10.1038/s41586-018-0002-9
Web of Sience KeyUT 000430082000040
関連URL isVersionOf https://doi.org/10.1038/s41586-018-0002-9
フルテキストURL Nat_Comm_9_2132.pdf
著者 Nishimura, Noriyuki| Tsuchiya, Wataru| Moresco, James J.| Hayashi, Yuki| Satoh, Kouji| Kaiwa, Nahomi| Irisa, Tomoko| Kinoshita, Toshinori| Schroeder, Julian I.| Yates III, John R.| Hirayama, Takashi| Yamazaki, Toshimasa|
抄録 Abscisic acid (ABA) regulates abiotic stress and developmental responses including regulation of seed dormancy to prevent seeds from germinating under unfavorable environmental conditions. ABA HYPERSENSITIVE GERMINATION1 (AHG1) encoding a type 2C protein phosphatase (PP2C) is a central negative regulator of ABA response in germination; however, the molecular function and regulation of AHG1 remain elusive. Here we report that AHG1 interacts with DELAY OF GERMINATION1 (DOG1), which is a pivotal positive regulator in seed dormancy. DOG1 acts upstream of AHG1 and impairs the PP2C activity of AHG1 in vitro. Furthermore, DOG1 has the ability to bind heme. Binding of DOG1 to AHG1 and heme are independent processes, but both are essential for DOG1 function in vivo. Our study demonstrates that AHG1 and DOG1 constitute an important regulatory system for seed dormancy and germination by integrating multiple environmental signals, in parallel with the PYL/RCAR ABA receptor-mediated regulatory system.
発行日 2018-06-06
出版物タイトル Nature Communications
9巻
出版者 Springer Nature
開始ページ 2132
ISSN 2041-1723
NCID AA12645905
資料タイプ 学術雑誌論文
言語 English
OAI-PMH Set 岡山大学
論文のバージョン publisher
PubMed ID 29875377
DOI 10.1038/s41467-018-04437-9
関連URL isVersionOf https://doi.org/10.1038/s41467-018-04437-9