The crystal structure of Deg9 reveals a novel octameric-type HtrA protease
文献类型：期刊论文
| 作者 | Ouyang, Min; Li, Xiaoyi; Zhao, Shun; Pu, Hua; Shen, Jianren4,5 ; Adam, Zach3; Clausen, Tim2; Zhang, Lixin6
|
| 刊名 | NATURE PLANTS
 |
| 出版日期 | 2017 |
| 卷号 | 3期号:12页码:973-982 |
| ISSN号 | 2055-026X |
| DOI | 10.1111/oik.04129 |
| 文献子类 | Article |
| 英文摘要 | The high temperature requirement A (HtrA) proteases (also termed Deg proteases) play important roles in diverse organisms by regulating protein quality and quantity. One of the 16 Arabidopsis homologs, Deg9, is located in the nucleus where it modulates cytokinin-and light-mediated signalling via degrading the ARABIDOPSIS RESPONSE REGULATOR 4 (ARR4). To uncover the structural features underlying the proteolytic activity of Deg9, we determined its crystal structure. Unlike the well-established trimeric building block of HtrAs, Deg9 displays a novel octameric structure consisting of two tetrameric rings that have distinct conformations. Based on the structural architecture, we generated several mutant variants of Deg9, determined their structure and tested their proteolytic activity towards ARR4. The results of the structural and biochemical analyses allowed us to propose a model for a novel mechanism of substrate recognition and activity regulation of Deg9. In this model, protease activation of one tetramer is mediated by en-bloc reorientation of the protease domains to open an entrance for the substrate in the opposite (inactive) tetramer. This study provides the structural basis for understanding how the levels of nuclear signal components are regulated by a plant protease. |
| 学科主题 | Environmental Sciences & Ecology |
| 出版地 | LONDON |
| 电子版国际标准刊号 | 2055-0278 |
| WOS关键词 | HUMAN BETA-TRYPTASE ; SERINE-PROTEASE ; SIGNAL-TRANSDUCTION ; QUALITY CONTROL ; PHOTOSYSTEM-II ; STRESS SENSOR ; PHYTOCHROME-B ; ACTIVE-SITE ; PDZ DOMAIN ; ARABIDOPSIS |
| 语种 | 英语 |
| WOS记录号 | WOS:000408908700003 |
| 出版者 | NATURE PUBLISHING GROUP |
| 资助机构 | Joint NSFC-ISF Research Program - National Natural Science Foundation of China [31661143026] ; Joint NSFC-ISF Research Program - Israel Science Foundation [31661143026] ; Strategic Priority Research Program of the Chinese Academy of SciencesChinese Academy of Sciences [XDB17000000] ; Youth Innovation Promotion Association CAS [2013059] |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/22265]  |
| 专题 | 中科院光生物学重点实验室 |
| 作者单位 | 1.Univ Chinese Acad Sci, Coll Life Sci, Beijing, Peoples R China 2.Hebrew Univ Jerusalem, Robert H Smith Inst Plant Sci & Genet Agr, Rehovot, Israel 3.Okayama Univ, Grad Sch Nat Sci & Technol, Okayama, Japan 4.Okayama Univ, Res Inst Interdisciplinary Sci, Okayama, Japan 5.Chinese Acad Sci, Inst Bot, Photosynth Res Ctr, Key Lab Photobiol, Beijing, Peoples R China 6.Res Inst Mol Pathol, Vienna, Austria |
| 推荐引用方式 GB/T 7714 | Ouyang, Min,Li, Xiaoyi,Zhao, Shun,et al. The crystal structure of Deg9 reveals a novel octameric-type HtrA protease[J]. NATURE PLANTS,2017,3(12):973-982. |
| APA | Ouyang, Min.,Li, Xiaoyi.,Zhao, Shun.,Pu, Hua.,Shen, Jianren.,...&Zhang, Lixin.(2017).The crystal structure of Deg9 reveals a novel octameric-type HtrA protease.NATURE PLANTS,3(12),973-982. |
| MLA | Ouyang, Min,et al."The crystal structure of Deg9 reveals a novel octameric-type HtrA protease".NATURE PLANTS 3.12(2017):973-982. |
入库方式： OAI收割
来源：植物研究所
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