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Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts

文献类型：期刊论文

作者Liu, Xi1; Liu, Shian2; Feng, Yingang3; Liu, Jian-Zhong4; Chen, Yuling1; Khanh Pham2; Deng, Haiteng1; Hirschi, Kendal D.2; Wang, Xinquan1; Cheng, Ninghui2
刊名PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
出版日期2013-06-04
卷号110期号:23页码:9565-9570
关键词reactive oxygen species nuclear magnetic resonance
中文摘要 Glutaredoxins (Grxs) have been identified across taxa as important mediators in various physiological functions.Achloroplasticmonothiol glutaredoxin,AtGRXS16 fromArabidopsis thaliana, comprises two distinct functional domains, an N-terminal domain (NTD) with GlyIleTyr- TyrIleGly (GIY-YIG) endonuclease motif and a C-terminal Grx module, to coordinate redox regulationandDNAcleavagein chloroplasts.Structural determination of AtGRXS16-NTD showed that it possesses a GIY– YIG endonuclease fold, but the critical residues for the nuclease activity are different from typical GIY–YIG endonucleases. AtGRXS16-NTDwas able to cleave λDNA and chloroplast genomic DNA, and the nuclease activity was significantly reduced in AtGRXS16. Functional analysis indicated that AtGRXS16-NTD could inhibit the ability of AtGRXS16 to suppress the sensitivity of yeast grx5 cells to oxidative stress; however, the C-terminal Grx domain itself and AtGRXS16 with a Cys123Ser mutation were active in these cells and able to functionally complement a Grx5 deficiency in yeast. Furthermore, the two functional domains were shown to be negatively regulated through the formation of an intramolecular disulfide bond. These findings unravel amanner of regulation for Grxs and provide insights into themechanistic link between redox regulation and DNA metabolism in chloroplasts.
 
英文摘要Glutaredoxins (Grxs) have been identified across taxa as important mediators in various physiological functions. A chloroplastic monothiol glutaredoxin, AtGRXS16 from Arabidopsis thaliana, comprises two distinct functional domains, an N-terminal domain (NTD) with GlyIleTyr-TyrIleGly (GIY-YIG) endonuclease motif and a C-terminal Grx module, to coordinate redox regulation and DNA cleavage in chloroplasts. Structural determination of AtGRXS16-NTD showed that it possesses a GIY-YIG endonuclease fold, but the critical residues for the nuclease activity are different from typical GIY-YIG endonucleases. AtGRXS16-NTD was able to cleave lambda DNA and chloroplast genomic DNA, and the nuclease activity was significantly reduced in AtGRXS16. Functional analysis indicated that AtGRXS16-NTD could inhibit the ability of AtGRXS16 to suppress the sensitivity of yeast grx5 cells to oxidative stress; however, the C-terminal Grx domain itself and AtGRXS16 with a Cys123Ser mutation were active in these cells and able to functionally complement a Grx5 deficiency in yeast. Furthermore, the two functional domains were shown to be negatively regulated through the formation of an intramolecular disulfide bond. These findings unravel a manner of regulation for Grxs and provide insights into the mechanistic link between redox regulation and DNA metabolism in chloroplasts.
WOS标题词Science & Technology
学科主题代谢物组学
类目[WOS]Multidisciplinary Sciences
研究领域[WOS]Science & Technology - Other Topics
关键词[WOS]IRON-SULFUR CLUSTER ; MONOTHIOL GLUTAREDOXIN ; OXIDATIVE STRESS ; I-TEVI ; TD INTRON ; REPAIR ; ENZYMES ; DOMAIN ; YEAST ; GRX5
收录类别SCI
语种英语
WOS记录号WOS:000320503000079
公开日期2014-03-24
源URL[http://ir.qibebt.ac.cn:8080/handle/337004/1681]  
专题青岛生物能源与过程研究所_代谢物组学团队
作者单位1.Tsinghua Univ, Sch Life Sci, Struct Biol Ctr, Minist Educ,Key Lab Prot Sci, Beijing 100084, Peoples R China
2.Baylor Coll Med, Dept Pediat, USDA ARS Children Nutr Res Ctr, Houston, TX 77030 USA
3.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Shandong Prov Key Lab Energy Genet, Qingdao 266101, Shandong, Peoples R China
4.Zhejiang Normal Univ, Coll Chem & Life Sci, Jinhua 321004, Zhejiang, Peoples R China
推荐引用方式
GB/T 7714		 Liu, Xi,Liu, Shian,Feng, Yingang,et al. Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2013,110(23):9565-9570.
APA Liu, Xi.,Liu, Shian.,Feng, Yingang.,Liu, Jian-Zhong.,Chen, Yuling.,...&Cheng, Ninghui.(2013).Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,110(23),9565-9570.
MLA Liu, Xi,et al."Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 110.23(2013):9565-9570.

入库方式： OAI收割

来源：青岛生物能源与过程研究所

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