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An effective system for detecting protein-protein interaction based on in vivo cleavage by PPV NIa protease

Protein & Cell 2012年第12期3卷 921-928页

作者： Nuoyan zheng Xiahe Huang Bojiao Yin Dan Wang Qi Xie Department of Nephrology the First Affiliated HospitalSun Yat-Sen UniversityGuangzhou 510000China Research Center of Translational Medicine the First Affiliated HospitalSun Yat-Sen UniversityGuangzhou 510000China State Key Laboratory of Plant Genomics National Centre for Plant Gene ResearchInstitute of Genetics and Developmental BiologyChinese Academy of SciencesBeijing 100101China Animal Center Institute of Genetics and Developmental BiologyChinese Academy of SciencesBeijing 100101China

Detection of protein-protein interaction can provide valuable information for investigating the biological function of *** current methods that applied in protein-protein interaction,such as co-immunoprecipitation and pull down etc.,often cause plenty of working time due to the burdensome cloning and puri-fication *** we established a system that characterization of protein-protein interaction was accomplished by co-expression and simply purification of target proteins from one expression cassette within *** *** modified pET vector into co-expression vector pInvivo which encoded PPV NIa protease,two cleavage site F and two multiple cloning sites that flanking cleavage *** target proteins(for example:protein A and protein B)were inserted at multiple cloning sites and translated into polyprotein in the order of MBP tag-protein A-site F-PPV NIa protease-site F-protein B-His6 *** NIa protease carried out intracellular cleavage along expression,then led to the separation of polyprotein components,therefore,the interaction between protein A-protein B can be detected through one-step purification and *** control for protein B was brought into this system for monitoring interaction *** successfully employed this system to prove two cases of reported protien-protein interaction:RHA2a/ANAC and FTA/*** conclusion,a convenient and efficient system has been successfully developed for detecting protein-protein interaction.

关键词： PPV NIa protease protein-protein interaction in vivo cleavage fusion protein

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Non-26S Proteasome Proteolytic Role of Ubiquitin in Plant Endocytosis and Endosomal Trafficking

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Journal of Integrative Plant Biology 2013年第1期55卷 54-63页

作者： Miaomiao Tian Qi Xie State Key Laboratory of Plant Genomics National Center for Plant Gene Research Institute of Genetics and Developmental Biologythe Chinese Academy of Sciences

The 76 amino acid protein ubiquitin （Ub） is highly conserved in all eukaryotic species. It plays important roles in many cellular processes by covalently attaching to the target proteins. The best known function of Ub is marking substrate proteins for degra- dation by the 26S proteasome. In fact, other consequences of ubiquitination have been discovered in yeast and mammals, such as membrane trafficking, DNA repair, chromatin modification, and protein kinase activation. The common mechanism underlying these processes is that Ub serves as a signal to sort proteins to the vacuoles or lysosomes for degradation as opposed to 26S proteasome-dependent degradation. To date, several reports have indicated that a similar function of Ub also exists in plants. This review focuses on a summary and analysis of the recent research progress on Ub acting as a signal to mediate endocytosis and endosomal trafficking in plants.

关键词： Endocytosis endosomal trafficking ubiquitin.

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The Ever Expanding Role of Ubiquitin and SUMO in Plant Biology

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Journal of Integrative Plant Biology 2013年第1期55卷 5-6页

作者： Giovanna Serino Qi Xie "Charles Darwin" Department of Biology and Biotechnology Sapienza Università di Roma Laboratory of Plant Molecular Signaling Institute of Genetics and Developmental Biology Chinese Academy of sciences

When it was discovered in the 1970s as a ubiquitous protein, ubiquitin, a 76-aminoacid peptide, had no assigned function. It was not until later that ubiquitin was found to be a necessary cofactor in a vital cellular process： the degradation of proteins. Work by Avram Hershko, Aaron Ciechanover, and Irwin Rose （for which they received the 2004 Nobel Prize in Chemistry） showed that the covalent attachment of ubiquitin provide pro-teins with a tag that dispatches them to the proteasome, the main cell degradation machinery （Ciechanover 2012）. Subsequent work, has revealed that ubiquitin belongs to a broader family of ubiquitin-like proteins that can modify not only protein stability, but also subcellular localization and function.

关键词： SUMO The Ever Expanding Role of Ubiquitin and SUMO in Plant Biology

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AtPUB19, a U-Box E3 Ubiquitin Ligase, Negatively Regulates Abscisic Acid and Drought Responses in Arabidopsis thaliana

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Molecular Plant 2011年第6期4卷 938-946页

作者： Yong-Chang Liu Yao-Rong Wu Xia-He Huang Jie Sun Qi Xie College of Agriculture/The Key Laboratory of Oasis Eco-agriculture Shihezi University Shihezi Xinjiang 832003 China State Key Laboratory of Plant Genomics National Center for Plant Gene Research Institute of Genetics and Developmental Biology Chinese Academy of Sciences Beijing 100101 China

Ubiquitination is an important protein post-translational modification, which is involved in various cellular processes in higher plants, and U-box E3 ligases play important roles in diverse functions in eukaryotes. Here, we describe the functions ofArabidopsis thaliana PUB19 （AtPUB19）, which we demonstrated in an in vitro assay to encode a U-box type E3 ubiquitin ligase. AtPUB19 was up-regulated by drought, salt, cold, and abscisic acid （ABA）. Down-regulation of AtPUB19 led to hypersensitivity to ABA, enhanced ABA-induced stomatal closing, and enhanced drought tolerance, while AtPUB19 overexpression resulted in the reverse phenotypes. Molecular analysis showed that the expression levels of a number of ABA and stress marker genes were altered in both AtPUB19 overexpressing and atpub19-1 mutant plants. In summary, our data show that AtPUB19 negatively regulates ABA and drought responses in A. thaliana.

关键词： U-box ABA drought stress Arabidopsis.

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Unfolded protein response activation compensates endoplasmic reticulum-associated degradation deficiency in Arabidopsis

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Journal of Integrative Plant Biology 2017年第7期59卷 506-521页

作者： Qingliang Li Hai Wei Lijing Liu Xiaoyuan Yang Xiansheng Zhang Qi Xie State Key Laboratory of Plant Genomics National Center for Plant Gene Research Institute of Genetics and Developmental Biology Chinese Academy of Sciences State Key Laboratory of Crop Biology Shandong Key Laboratory of Crop Biology College of Life Sciences Shandong Agricultural University

Abiotic stresses often disrupt protein folding and induce endoplasmic reticulum （ER） stress. There is a sophisticated ER quality control （ERQC） system to mitigate the effects of malfunctioning proteins and maintain ER homeostasis. The accumulation of misfolded proteins in the ER activates the unfolded protein response （UPR） to enhance ER protein folding and the degradation of misfolded proteins mediate by ER- associated degradation （ERAD）. That ERQC reduces abiotic stress damage has been well studied in mammals and yeast. However, in plants, both ERAD and UPR have been studied separately and found to be critical for plant abiotic stress tolerance. In this study, we discovered that UPR-associated transcription factors AtbZlP17, AtbZIP28 and AtbZIP60 responded to tunicamycin （TM） and NaCl induced ER stress and subsequently enhanced Arabidopsis thaliana abiotic stress tolerance. They regulated the expression level of ER chaperones and the HRD1-complex components. Moreover, overexpression of AtbZIP17, AtbZIP28 and AtbZIP60 could restore stress tolerance via ERAD in the HRD1-complex mutant hrd3a-2, which suggested that UPR and ERAD have an interactive mechanism in Arabidopsts.

关键词： ZIP ERAD HRD in of UPR

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Generation of glyco-engineered BY2 cell lines with decreased expression of plant-specific glycoepitopes

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Protein & Cell 2011年第1期2卷 41-47页

作者： Bo-jiao Yin Ting Gao Nuo-yan Zheng Yin Li San-yuan Tang Li-ming Liang Qi XIE State Key Laboratory of Plant Genomics National Center for Plant Gene ResearchInstitute of Genetics and Developmental BiologyChinese Academy of SciencesDatun RoadBeijing 100101China State Key Laboratory of Biocontrol School of Life SciencesSun Yat-sen(Zhongshan)University135 Xingang Road WGuangzhou 510275China

Plants are known to be efficient hosts for the production of mammalian therapeutic ***,plants produce complex N-glycans bearingβ1,2-xylose and coreα1,3-fucose residues,which are absent in *** immunogenicity and allergenicity of plant-specific Nglycans is a key concern in mammalian *** this study,we amplified the sequences of 2 plant-specific glycosyltransferases from Nicotiana tabacum *** Bright Yellow 2(BY2),which is a well-established cell line widely used for the expression of therapeutic *** expression of the endogenous xylosyltranferase(XylT)and fucosyltransferase(FucT)was downregulated by using RNA interference(RNAi)*** xylosylated and core fucosylated N-glycans were significantly,but not completely,reduced in the glycoengineered ***,these RNAi-treated cell lines were stable and viable and did not exhibit any obvious ***,this study may provide an effective and promising strategy to produce recombinant glycoproteins in BY2 cells with humanized N-glycoforms to avoid potential immunogenicity.

关键词： BY2 cells N-glycosylation glycosyltransferase RNA interference

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UBC32 Mediated Oxidative Tolerance in Arabidopsis

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Journal of Genetics and Genomics 2012年第8期39卷 415-417页

作者： Feng Cui Lijing Liu Qingliang Li Chengwei Yang Qi Xie State Key Laboratory of Plant Genomics National Center for Plant Gene Research Institute of Genetics and Developmental Biology Chinese Academy of Sciences Beijing 100101 China Guangdong Key Lab of Biotechnology for Plant Development College of Life Science South China Normal University Guangzhou 510631 China

Extreme environments such as salt stress often increase the reactive oxygen species （ROS） levels （Abogadallah, 2010; Miller et al., 2010）, which cause protein denaturation and damage （Kelsen et al., 2008）. In eukaryotic cells, the endo- plasmic reticulum （ER） lumen is highly oxidative environment, which help newly synthesized proteins form intermolecular or intramolecular disulfide bonds between their cysteine residues. However, the ROS must be regulated according to the folding load to protect the cell from the consequences of oxidative folding.

关键词： reactive oxygen species endoplasmic reticulum protein denaturation salt stress

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