The crystal structure of Deg9 reveals a novel octameric-type HtrA protease

doi:10.1111/oik.04129

CORC > 植物研究所 > 中国科学院植物研究所 > 中科院光生物学重点实验室

	The crystal structure of Deg9 reveals a novel octameric-type HtrA protease
	Ouyang, Min ; Li, Xiaoyi ; Zhao, Shun ; Pu, Hua ; Shen, Jianren 4,5; Adam, Zach 1; Clausen, Tim 2; Zhang, Lixin 3
刊名	NATURE PLANTS
	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
电子版国际标准刊号	2055-0278
出版地	LONDON
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
出版者	NATURE PUBLISHING GROUP
WOS记录号	WOS:000408908700003
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]
内容类型	期刊论文
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.Okayama Univ, Grad Sch Nat Sci & Technol, Okayama, Japan 2.Hebrew Univ Jerusalem, Robert H Smith Inst Plant Sci & Genet Agr, Rehovot, Israel 3.Res Inst Mol Pathol, Vienna, Austria 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.Univ Chinese Acad Sci, Coll Life Sci, Beijing, Peoples R China
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.