An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins
文献类型：期刊论文
| 作者 | Tani, Kazutoshi; Kanno, Ryo; Kurosawa, Keigo; Takaichi, Shinichi5; Nagashima, Kenji V. P.; Hall, Malgorzata; Yu, Long-Jiang; Kimura, Yukihiro1; Madigan, Michael T.; Mizoguchi, Akira |
| 刊名 | COMMUNICATIONS BIOLOGY
 |
| 出版日期 | 2022 |
| 卷号 | 5期号:1 |
| DOI | 10.1038/s42003-022-04174-2 |
| 文献子类 | Article |
| 英文摘要 | The cryo-EM structure of the unusual light-harvesting 1-reaction center (LH1-RC) complex from Rpi. globiformis, the most acidophilic anaerobic purple bacteria, is presented, characterized and compared to other photosynthetic bacteria. Rhodopila globiformis is the most acidophilic of anaerobic purple phototrophs, growing optimally in culture at pH 5. Here we present a cryo-EM structure of the light-harvesting 1-reaction center (LH1-RC) complex from Rhodopila globiformis at 2.24 angstrom resolution. All purple bacterial cytochrome (Cyt, encoded by the gene pufC) subunit-associated RCs with known structures have their N-termini truncated. By contrast, the Rhodopila globiformis RC contains a full-length tetra-heme Cyt with its N-terminus embedded in the membrane forming an alpha-helix as the membrane anchor. Comparison of the N-terminal regions of the Cyt with PufX polypeptides widely distributed in Rhodobacter species reveals significant structural similarities, supporting a longstanding hypothesis that PufX is phylogenetically related to the N-terminus of the RC-bound Cyt subunit and that a common ancestor of phototrophic Proteobacteria contained a full-length tetra-heme Cyt subunit that evolved independently through partial deletions of its pufC gene. Eleven copies of a novel gamma-like polypeptide were also identified in the bacteriochlorophyll a-containing Rhodopila globiformis LH1 complex; gamma-polypeptides have previously been found only in the LH1 of bacteriochlorophyll b-containing species. These features are discussed in relation to their predicted functions of stabilizing the LH1 structure and regulating quinone transport under the warm acidic conditions. |
| 学科主题 | Biology ; Multidisciplinary Sciences |
| 电子版国际标准刊号 | 2399-3642 |
| 出版地 | BERLIN |
| WOS关键词 | CRYO-EM STRUCTURE ; RHODOPSEUDOMONAS-VIRIDIS ; CYTOCHROME SUBUNIT ; CORE COMPLEX ; PUF OPERON ; GLOBIFORMIS ; SEQUENCES ; EXPRESSION ; FEATURES ; RUBRUM |
| WOS研究方向 | Science Citation Index Expanded (SCI-EXPANDED) |
| 语种 | 英语 |
| 出版者 | NATURE PORTFOLIO |
| WOS记录号 | WOS:000879788300005 |
| 资助机构 | Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from AMED [JP20am0101118, 1758, JP20am0101116, 1878, 17am0101116j0001, 18am0101116j0002, 19am0101116j0003, 22am121004] ; Okinawa Institute of Science and Technology (OIST), Scientific Computing & Data Analysis Section at OIST ; Japanese Cabinet Office ; National Key R&D Program of China [2021YFA0909600] ; JSPS KAKENHI [JP16H04174, JP18H05153, JP20H05086, JP20H02856] ; Takeda Science Foundation ; Kurata Memorial Hitachi Science and Technology Foundation, Japan |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/28761]  |
| 专题 | 中科院光生物学重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Photosynth Res Ctr, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China 2.Madigan, Michael T.] Southern Illinois Univ, Sch Biol Sci, Dept Microbiol, Carbondale, IL 62901 USA 3.Mie Univ, Grad Sch Med, Tsu, Mie 5148507, Japan 4.Kanno, Ryo; Hall, Malgorzata; Humbel, Bruno M.] Okinawa Inst Sci & Technol Grad Univ OIST, Res Support Div, Imaging Sect, 1919-1 Tancha, Onna Son, Okinawa 9040495, Japan 5.Ibaraki Univ, Fac Sci, Mito, Ibaraki 3108512, Japan 6.Tokyo Univ Agr, Fac Sci, Dept Mol Microbiol, Setagaya Ku, Tokyo 1568502, Japan 7.Nagashima, Kenji V. P.] Kanagawa Univ, Res Inst Integrated Sci, 2946 Tsuchiya, Hiratsuka, Kanagawa 2591293, Japan 8.Kobe Univ, Grad Sch Agr, Dept Agrobiosci, Kobe, Hyogo 6578501, Japan |
| 推荐引用方式 GB/T 7714 | Tani, Kazutoshi,Kanno, Ryo,Kurosawa, Keigo,et al. An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins[J]. COMMUNICATIONS BIOLOGY,2022,5(1). |
| APA | Tani, Kazutoshi.,Kanno, Ryo.,Kurosawa, Keigo.,Takaichi, Shinichi.,Nagashima, Kenji V. P..,...&Wang-Otomo, Zheng-Yu.(2022).An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins.COMMUNICATIONS BIOLOGY,5(1). |
| MLA | Tani, Kazutoshi,et al."An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins".COMMUNICATIONS BIOLOGY 5.1(2022). |
入库方式： OAI收割
来源：植物研究所
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