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| The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein | |
| Fang, Ying1; Zhao, Shun1; Zhang, Feilong2; Zhao, Aiguo3; Zhang, Wenxia; Zhang, Min2; Liu, Lin | |
| 2016 | |
| Source Publication | SCIENTIFIC REPORTS
 |
| ISSN | 2045-2322 |
| Volume | 6 |
| Abstract | Tetrapyrrole biosynthesis is an essential and tightly regulated process, and glutamyl-tRNA reductase (GluTR) is a key target for multiple regulatory factors at the post-translational level. By binding to the thylakoid membrane protein FLUORESCENT (FLU) or the soluble stromal GluTR-binding protein (GBP), the activity of GluTR is down-or up-regulated. Here, we reconstructed a ternary complex composed of the C-terminal tetratricopepetide-repeat domain of FLU, GBP, and GluTR, crystallized and solved the structure of the complex at 3.2 angstrom. The overall structure resembles the shape of merged two binary complexes as previously reported, and shows a large conformational change within GluTR. We also demonstrated that GluTR binds tightly with GBP but does not bind to GSAM under the same condition. These findings allow us to suggest a biological role of the ternary complex for the regulation of plant GluTR. |
| Subject Area | Multidisciplinary Sciences |
| DOI | 10.1038/srep19756 |
| Indexed By | SCI |
| Language | 英语 |
| WOS Keyword | 5-AMINOLEVULINIC ACID SYNTHESIS ; TETRAPYRROLE BIOSYNTHESIS ; CHLOROPHYLL BIOSYNTHESIS ; NEGATIVE REGULATOR ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; ENZYME ; EXPRESSION ; THALIANA ; HEMA1 |
| WOS Research Area | Science Citation Index Expanded (SCI-EXPANDED) |
| WOS ID | WOS:000368667700002 |
| Publisher | NATURE PUBLISHING GROUP |
| Subtype | Article |
| Publication Place | LONDON |
| Funding Organization | National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31370759, 31500243] ; National Basic Research Program of ChinaNational Basic Research Program of China [2011CBA00901] ; CASChinese Academy of Sciences [KGZD-EW-T05] |
| Corresponding Author Email | liulin@ibcas.ac.cn |
| OA | gold, Green Published |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.ibcas.ac.cn/handle/2S10CLM1/25326 |
| Collection | 中科院光生物学重点实验室 |
| Affiliation | 1.Chinese Acad Sci, Inst Bot, CAS Ctr Excellence Mol Plant Sci, Key Lab Photobiol, Beijing 100093, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Anhui Univ, Sch Life Sci, Hefei 230601, Anhui, Peoples R China 4.Northwest A&F Univ, Coll Life Sci, Xian 712100, Shaanxi, Peoples R China |
| Recommended Citation GB/T 7714 | Fang, Ying,Zhao, Shun,Zhang, Feilong,et al. The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein[J]. SCIENTIFIC REPORTS,2016,6. |
| APA | Fang, Ying.,Zhao, Shun.,Zhang, Feilong.,Zhao, Aiguo.,Zhang, Wenxia.,...&Liu, Lin.(2016).The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein.SCIENTIFIC REPORTS,6. |
| MLA | Fang, Ying,et al."The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein".SCIENTIFIC REPORTS 6(2016). |
| Files in This Item: | ||||||
| File Name/Size | DocType | Version | Access | License | ||
| Fang-2016-The Arabid（2792KB） | 期刊论文 | 出版稿 | 开放获取 | CC BY-NC-SA | View Application Full Text | |
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