Advances in Research on Plant Ubiquitin Genes

doi:10.11924/j.issn.1000-6850.casb20190500148

Abstract

Abstract:

In this paper, the composition of the ubiquitin proteasome system, the structure of monoubiquitin, polyubiquitin, and ubiquitin-like gene and the role of ubiquitin system in plant growth and development, and the function of E3 ligase in response to biotic and abiotic stress were reviewed. In view of the existing related research, it is proposed that there are few studies on the target protein itself, few reports on the HECT family of E3 ligase, and the timing site of E3 regulatory network and ubiquitination is still unclear. The future research on ubiquitin, such as strengthening the research on cloning related genes and gene interaction, strengthening the research on target protein information and E3 molecular mechanism, is expected to provide references for the research on plant ubiquitin system, the structure and function of ubiquitin genes.

Key words: plant, ubiquitination, gene structure, E3 ubiquitin ligase, growth and stress

CLC Number:

Wang Yixi, Yu Bingwei, Yan Shuangshuang, Qiu Zhengkun, Chen Changming, Lei Jianjun, Tian Shibing, Cao Bihao. Advances in Research on Plant Ubiquitin Genes[J]. Chinese Agricultural Science Bulletin, 2020, 36(20): 14-22.

References 108

[1]	Goldstein G, Scheid M, Hammerling V, et al. Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells[J]. Proceedings of the National Academy of Sciences of the United States of America, 1975,72(1):11-15. doi: 10.1073/pnas.72.1.11 URL pmid: 1078892
[2]	Von Gerbrand J H N, Huib Ovaa. How to Target Viral and Bacterial Effector Proteins Interfering with Ubiquitin Signaling[A].// Compans R W, Malissen B, Aktories K, et al. Current Topics in Microbiology and Immunology[C]. Springer Verlag, Berlin, Germany, 2018.
[3]	Pickart C M, Fushman D. Polyubiquitin chains: polymeric protein signals[J]. Current Opinion in ChemicalBiology, 2004,8(6):610-616.
[4]	Rowland O, Ludwig A A, Merrick C J, et al. Functional analysis of Avr9/Cf-9 rapidly elicited genes identifies a protein kinase, ACIK1, that is essential for full Cf-9-dependent disease resistance in tomato[J]. The Plant cell, 2005,17(1):295-310. URL pmid: 15598806
[5]	Kraft E, Stone SL, Ma L, et al. Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis[J]. Plant physiology, 2005,139(4):1597-1611. doi: 10.1104/pp.105.067983 URL pmid: 16339806
[6]	Vierstra R D. The ubiquitin-26S proteasome system at the nexus of plant biology[J]. Nature Review Molecular Cell Biology, 2009,10(6):385-397.
[7]	Shu K, Yang W. E3 ubiquitin ligases: ubiquitous actors in plant development and abiotic stress responses[J]. Plant & Cell Physiology, 2017,58(9):1461-1476. URL pmid: 28541504
[8]	Thomann A, Brukhin V, Dieterle M, et al. Arabidopsis CUL3A and CUL3B genes are essential for normal embryogenesis[J]. The Plant Journal, 2005,43(3):437-448. doi: 10.1111/j.1365-313X.2005.02467.x URL pmid: 16045478
[9]	裴宝嘉. 组蛋白单泛素化参与拟南芥抗大丽轮枝菌毒素防卫反应的机理研究[D]. 北京: 中国农业大学, 2014.
[10]	Chih-Wen Sun, Judy Callis. Independent modulation of Arabidopsis thaliana polyubiquitin mRNAs in different organs and in response to environmental changes[J]. The Plant Journal, 1997,11(5):1017-1027. doi: 10.1046/j.1365-313x.1997.11051017.x URL pmid: 9193073
[11]	Pokhilko A, Ramos J A, Holtan H, et al. Ubiquitin ligase switch in plant photomorphogenesis: A hypojournal[J]. Journal of theoretical biology, 2011,270(1):31-41. doi: 10.1016/j.jtbi.2010.11.021 URL pmid: 21093457
[12]	Adams E H S, Spoel S H. The ubiquitin-proteasome systemas a transcriptional regulator of plant immunity[J]. Journal of Experimental Botany, 2018,69(19):4529-4537. URL pmid: 29873762
[13]	Mazzucotelli E, Belloni S, Marone D, et al. The E3 ubiquitin ligase gene family in plants: regulation by degradation[J]. Current Genomics, 2006,7(8):509-522. doi: 10.2174/138920206779315728 URL pmid: 18369404
[14]	Thrower J S, Hoffman L, Rechsteiner M, et al. Recognition of the polyubiquitin proteolytic signal[J]. The EMBO journal, 2000,19(1):94-102. doi: 10.1093/emboj/19.1.94 URL pmid: 10619848
[15]	Dreher K, Callis J. Ubiquitin, hormones and biotic stress in plants[J]. Annals of botany, 2007,99(5):787-822. doi: 10.1093/aob/mcl255 URL pmid: 17220175
[16]	Callis J, Carpenter T, Sun C W, et al. Structure and Evolution of Genes Encoding Polyubiquitin and Ubiquitin-like Proteins in Arabidopsis Thaliana Ecotype Columbia[J]. Genetics, 1995,139(2):921-939. URL pmid: 7713442
[17]	Kirkpatrick D S, Hathaway N A, Hanna J, et al. Quantitative analysis of in vitro ubiquitinated cyclin B1reveals complex chain topology[J]. Nature Cell Biology, 2006,8(7):700-710. doi: 10.1038/ncb1436 URL pmid: 16799550
[18]	Kim HT, Kim KP, Lledias F, et al. GoldbergCertain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages[J]. the Journal of Biological Chemistry, 2007,282(24):17375-17386. doi: 10.1074/jbc.M609659200 URL pmid: 17426036
[19]	Mukhopadhyay D, Riezman H. Proteasome-independent functions of ubiquitin in endocytosis and signaling[J]. Science, 2007,315:201-205. URL pmid: 17218518
[20]	Richard D. Vierstra. Proteolysis in plants: mechanisms and functions[J]. Plant molecular biology, 1996,32(1-2):275-302. doi: 10.1007/BF00039386 URL pmid: 8980483
[21]	David Hondred, Walker Joseph M, Dennis E, et al. Use of ubiquitin fusions to augment protein expression in transgenic plants[J]. Plant physiology, 1999,119(2):713-724. URL pmid: 9952468
[22]	Hatfield Peggy M, Gosink Mark M, Carpenter Tami B, et al. The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana[J]. The Plant journal: for cell and molecular biology, 1997,11(2):213-226. doi: 10.1046/j.1365-313X.1997.11020213.x URL
[23]	Takizawa M, Goto A, Watanabe Y. The tobacco ubiquitin-activating enzymes NtE1A and NtE1B are induced by tobacco mosaic virus, wounding and stress hormones[J]. Molecular & Cells, 2005,19(2):228-231.
[24]	Zhang C, Song L, Choudhary M K, et al. Genome-wide analysis of genes encoding core components of the ubiquitin system in soybean (Glycine max) reveals a potential role for ubiquitination in host immunity against soybean cyst nematode[J]. BMC Plant Biology, 2018,18(1):149. doi: 10.1186/s12870-018-1365-7 URL pmid: 30021519
[25]	Imura Y, Molho M, Chuang C, et al. Cellular Ubc2/Rad6 E2 ubiquitin-conjugating enzyme facilitates tombusvirus replication in yeast and plants[J]. Virology, 2015,484(1):265-275. doi: 10.1016/j.virol.2015.05.022 URL
[26]	Jentsch S. The ubiquitin-conjugation system[J]. Annual Review of Genetics, 1992,26(1):179-207.
[27]	Windheim M, Peggie M, Cohen P, et al. Two different classes of E2 ubiquitin-conjugating enzymes are required for the monoubiquitination of proteins and elongation by polyubiquitin chains with a specific topology[J]. Biochemical Journal, 2008,409(3):723-729. doi: 10.1042/BJ20071338 URL pmid: 18042044
[28]	Hoege C, Pfander B, Moldovan G L, et al. RAD6-dependent DNA repairis linked to modification of PCNA by ubiquitin and SUMO[J]. Nature, 2002,419:135-141. doi: 10.1038/nature00991 URL pmid: 12226657
[29]	Smalle J, Vierstra R D. The ubiquitin 26S proteasome proteolytic pathway[J]. Annual Review of Plant Biology, 2004,55(1):555-590. doi: 10.1146/annurev.arplant.55.031903.141801 URL
[30]	Lin W Y, Lin S I, Chiou T J. Molecular regulators of phosphate homeostasis in plants[J]. Journal of Experimental Botany, 2009,60(5):1427-1438. doi: 10.1093/jxb/ern303 URL pmid: 19168668
[31]	Picker C M, Eddins M J. Ubiquitin: structures, functions, mechanisms[J]. Biochimica Et Biophysica Acta, 2004,1695(1-3):55-72. doi: 10.1016/j.bbamcr.2004.09.019 URL pmid: 15571809
[32]	贾琪, 孙松, 孙天昊, 等. F-box蛋白家族在植物抗逆响应中的作用机制[J]. 中国生态农业学报, 2018,26(8):1125-1136.
[33]	许克恒, 张云彤, 张莹, 等. 植物F-box基因家族的研究进展[J]. 生物技术通报, 2018,34(1):26-32.
[34]	Huibregtse J M, Scheffner M, Beaudenon S, et al. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase[J]. Proceedings of the National Academy of Sciences of the United States of America, 1995,92(11):2563-2567.
[35]	Downes B, Vierstra R D. Post-translational regulation in plants employing a diverse set of polypeptide tags[J]. Biochem Soc Trans, 2005,33(2):393-399.
[36]	Stone SL, Hauksdottir H, Troy A, et al. Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis[J]. Plant Physiology, 2005,137(1):13-30. doi: 10.1104/pp.104.052423 URL pmid: 15644464
[37]	胡婷丽, 李魏, 刘雄伦, 等. 泛素化在植物抗病中的作用[J]. 微生物学通报, 2014,41(6):1175-1179.
[38]	Aravind L, Koonin E V. The U box is a modified RING finger-acommon domain in ubiquitination[J]. Current Biology, 2000,10(4):132-134.
[39]	Azevedo C, Santos-Rosa M J, Shirasu K., The U-box protein family in plants[J]. Trends in plant science, 2001,6(8):354-358. doi: 10.1016/s1360-1385(01)01960-4 URL pmid: 11495788
[40]	Downes B P, Stupar R M, Gingerich D J, et al. The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis:UPL3 has a specific role in trichome development[J]. The Plant journal, 2003,35(6):729-742. doi: 10.1046/j.1365-313x.2003.01844.x URL pmid: 12969426
[41]	Freemont P S. The RING finger, A novel protein sequence motif related to the zinc finger[J]. Annals of the New York Academy of Sciences, 1993,684(1):174-192.
[42]	Lyzenga W J, Stone S L. Abiotic stress tolerance mediated by protein ubiquitination[J]. Journal of experimental botany, 2012,63(2):599-616. doi: 10.1093/jxb/err310 URL pmid: 22016431
[43]	Attaix D, Combaret L, Pouch M N, et al. Cellular control of ubiquitin-proteasome-dependent proteolysis[J]. Journal of Animal Science, 2002,80(2):E56-E63. doi: 10.2527/animalsci2002.80E-Suppl_2E56x URL
[44]	陈正凯. 家奏泛素基因的多态性与野蚕泛素基因的克隆及原核表达[D]. 兰州:兰州大学, 2007.
[45]	赵付安, 房卫平, 杨晓杰, 等. 陆地棉GhSUMO基因的克隆与黄萎病菌诱导表达分析[J]. 广西农业生物科学, 2011,30(4):359-364.
[46]	Gausing K, Barkardottir R. Structure and expression of ubiquitin genes in higher plants[J]. European journal of biochemistry, 1986,158(1):57-62. doi: 10.1111/j.1432-1033.1986.tb09720.x URL pmid: 2426105
[47]	Wang J L, Jiang J D, Oard J H. Structure expression and promoter activity of two polyubiquitin genes from rice (Oryza sativa L.)[J]. Plant Science, 2000,156(2):201-211. doi: 10.1016/s0168-9452(00)00255-7 URL pmid: 10936527
[48]	Wei H, Wang M L, Moore P H, et al. Comparative expression analysis of two sugarcane polyubiquitin promoters and flanking sequences in transgenic plants[J]. Journal of plant physiology, 2003,160(10):1241-1251. doi: 10.1078/0176-1617-01086 URL pmid: 14610893
[49]	Nenoi M, Mita K, Ichimura S, et al. Novel structure of a Chinese hamster polyubiquitin gene[J], Biochimica Biophysica Acta(BBA), 1994,1204(2):271-278.
[50]	Schiedlmeier B, Schmitt R. Repetitious structure and transcription control of a polyubiquitin gene in Volvox carteri[J]. Current Genetics, 1994,25(2):169-177. doi: 10.1007/BF00309544 URL pmid: 8087887
[51]	陆小平, 肖靓, 陈正凯, 等. 桑树多聚泛素基因的克隆及序列分析[J]. 蚕业科学, 2006,32(3):301-306.
[52]	Sharp Paul M, Li Wen-Hsiung. Ubiquitin genes as a paradigm of concerted evolution of tandem repeats[J]. Journal of molecular evolution, 1987,25(1):58-64. doi: 10.1007/BF02100041 URL pmid: 3041010
[53]	Christensen A H, Quail P H. Ubiquitin promoterbased vectors for high-level expression of selectable and/or screenable marker genes in monocotyledonous plants[J]. Transgenic Research, 1996,5(3):213-218. doi: 10.1007/BF01969712 URL pmid: 8673150
[54]	Marie-Noëlle Binet, acques-Henry Weil, Luc-Henri Tessier. Structure and expression of sunflower ubiquitin genes[J]. Plant molecular biology, 1991,17(3):395-407. doi: 10.1007/BF00040634 URL pmid: 1653059
[55]	Christensen A H, Sharrock R A, Quail P H. Maize polyubiquitin genes: structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer to protoplasts by electroporation[J]. Plant molecular biology, 1992,18(4):675-689. doi: 10.1007/BF00020010 URL pmid: 1313711
[56]	杨春. 条斑紫菜多聚泛素基因的克隆与系统进化分析[D]. 青岛:中国海洋大学, 2007.
[57]	解光宁. 玉米泛素受体ZmDA1、ZmDAR1对籽粒发育的影响[D]. 济南:山东大学, 2017.
[58]	Xia T, Li N, Jack D, et al. The Ubiquitin Receptor DA1 Interacts with the E3 Ubiquitin Ligase DA2 to Regulate Seed and Organ Size in Arabidopsis[J]. The Plant Cell, 2013,25(9):3347-3359. doi: 10.1105/tpc.113.115063 URL pmid: 24045020
[59]	Du L, Na Li, Chen L L, et al. The Ubiquitin Receptor DA1 Regulates Seed and Organ Size by Modulating the Stability of the Ubiquitin-Specific Protease UBP15/SOD2 in Arabidopsis[J]. The Plant Cell, 2014,26(2):665-677. doi: 10.1105/tpc.114.122663 URL pmid: 24585836
[60]	Criqui M C, de Almeida Engler J, Camasses A, et al. Molecular Characterization of Plant Ubiquitin-Conjugating Enzymes Belonging to the UbcP4/E2-C/UBCx/UbcH10 Gene Family[J]. Molecular Characterization of Arabidopsis UBC Genes, 2002,130(3):1230-1240.
[61]	Kinoshita A A, ten Hove C, Tabata R, et al. A plant U-box protein, PUB4, regulates asymmetric cell division and cell proliferation in the root meristem[J]. The Company of Biologists, 2015,142(3):444-453.
[62]	李魏. 拟南芥U-box蛋白PUB13的功能研究[D]. 长沙:湖南农业大学, 2012.
[63]	陈浩东. E3泛素连接酶SCFEBF1/2通过降解PIF3促进植物的光形态建成[J]. 当代生物学, 2017,27(16):2420-2430.
[64]	王琴. 拟南芥CRY2调控光形态建成的分子遗传学与生化分析[D]. 长沙:湖南大学, 2013.
[65]	王娟. 泛素-蛋白酶体相关调节因子CSN5B和OsEIP1的功能分析[D]. 北京:中国农业科学院, 2013.
[66]	周晓琳. 泛素连接酶基因GhATL86在棉花纤维发育中的功能研究[D]. 武汉:华中农业大学, 2017.
[67]	Goldberg A L. Protein degradation and protection against misfolded or damaged proteins[J]. Nature, 2003,426:895-899. doi: 10.1038/nature02263 URL pmid: 14685250
[68]	Marino D, Peeters N, Rivas S. Ubiquitination during plant immune signaling[J]. Plant Physioogyl, 2012,160(1):15-27.
[69]	Raúl E. Salinas-Mondragón, Cristina Garcidueñas-Piña, Plinio Guzmán. Early elicitor induction in members of a novel multigene family coding for highly related RING-H2 proteins in Arabidopsis thaliana[J]. Plant molecular biology, 1999,40(4):579-590. doi: 10.1023/a:1006267201855 URL pmid: 10480382
[70]	Molnar G, Bancos S, Nagy F, et al. Characterisation of BRH1, a brassinosteroid-responsive RING-H2 gene from Arabidopsis thaliana[J]. Planta, 2002,215(1):127-133. URL pmid: 12012249
[71]	Takai R, Matsuda N, Nakano A, et al. EL5, a rice N-acetylchito oligosaccharide elicitor responsive RING-H2 finger protein, is a ubiquitin ligase which functions in vitro in cooperation with an elicitor-responsive ubiquitin-conjugating enzyme, OsUBC5b[J]. Plant Journal, 2000,30(4):447-455. doi: 10.1046/j.1365-313x.2002.01299.x URL pmid: 12028574
[72]	Serrano M, Guzmán P. Isolation and gene expression analysis of Arabidopsis thaliana mutants with constitutive expression of ATL2, an early elicitor-response RING-H2 zinc-finger gene[J]. Genetics, 2004,167(2):919-929. doi: 10.1534/genetics.104.028043 URL pmid: 15238540
[73]	Trujillo M, Shirasu K. Ubiquitination in plant immunity[J]. Current Opinion in Plant Biology, 2010,13(4):402-408. doi: 10.1016/j.pbi.2010.04.002 URL pmid: 20471305
[74]	Marino D, Froidure S, Canonne J, et al. Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the transcription factor MYB30 weakening plant defence[J]. Nature Communications, 2013,4:1476. doi: 10.1038/ncomms2479 URL pmid: 23403577
[75]	He Q McLellan H, Boevink P C, et al. U-box E3 ubiquitin ligase PUB17 acts in the nucleus to promote specific immune pathways triggered by Phytophthora infestans[J]. Journal of experimental botany, 2015,66(11):3189-3199. doi: 10.1093/jxb/erv128 URL pmid: 25873665
[76]	Shen Q, Hu T, Bao M, et al. Tobacco RING E3 ligase NtRFP1 mediates ubiquitination and proteasomal degradation of a geminivirus-encoded betaC[J]. Molecular Plant, 2016,9(6):911-925. doi: 10.1016/j.molp.2016.03.008 URL pmid: 27018391
[77]	Ghannam A, Jacques A, de Ruffray P, et al. NtRING1, putative RING-finger E3 ligase protein, is a positive regulator of the early stages of elicitin-induced HR in tobacco[J]. Plant cell reports, 2016,35(2):415-428. doi: 10.1007/s00299-015-1893-7 URL pmid: 26542819
[78]	Yu Y, Xu W, Wang J, et al. The Chinese wild grapevine (Vitis pseudoreticulata) E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) activates plant defense responses by inducing proteolysis of the VpWRKY11 transcription factor[J]. New Phytol, 2013,200(3):834-846. doi: 10.1111/nph.12418 URL pmid: 23905547
[79]	姚文孔. 中国野生华东葡萄泛素连接酶基因VpPUB24功能研究[D]. 杨凌:西北农林科技大学, 2017.
[80]	Heise A, Lippok B, Kirsch C, et al. Two immediateearly pathogen-responsive members of the AtCMPG gene family in Arabidopsis thaliana and the W-box-containing elicitor-response element of AtCMPG1[J]. Proceedings of the National Academy of Sciences of the United States of America, 2002,99(13):9049-9054. doi: 10.1073/pnas.132277699 URL pmid: 12084942
[81]	Sahu P P, Sharma N, Puranik S, et al. Tomato 26S Proteasome subunit RPT4 a regulates ToLCNDV transcription and activates hypersensitive response in tomato[J]. Scientific Reports, 2016,6(1):270-278.
[82]	余仲夏. 去泛素化酶复合体USP1-UAF1在抗病毒固有免疫反应中的作用及分子机制[D]. 济南:山东大学, 2017.
[83]	Thais H R, Shugo M, Takeo S, et al. The Arabidopsis ubiquitin ligase ATL31 is transcriptionally controlled by WRKY33 transcription factor in response to pathogen attack[J]. Plant Biotechnology, 2015,32(1):11-19. doi: 10.5511/plantbiotechnology.14.1201b URL
[84]	Zeng LR, Qu S, Bordeos A, et al. Spotted leaf11, a negative regulator of plant cell death and defense, encodes a U-box/armadillo repeat protein endowed with E3 ubiquitin ligase activity[J]. The Plant cell, 2004,16(10):2795-2808. doi: 10.1105/tpc.104.025171 URL pmid: 15377756
[85]	Liu JL, Park CH, He F, et al. The RhoGAP SPIN6 Associates with SPL11 and OsRac1 and Negatively Regulates Programmed Cell Death and Innate Immunity in Ricep[J]. Public Library of Science, 2015,11(2):1-23.
[86]	Sakuma Y, Maruyama K, Qin F, et al. Dual function of an Arabidopsis transcription factor DREB2A in water-stress-responsive and heatstress-responsive gene expression[J]. Proceedings of the National Academy of Sciences of the United States of America, 2006,103(49):18822-18827. URL pmid: 17030801
[87]	Qin F, Sakuma Y, Tran L S, et al. Arabidopsis DREB2A-interacting proteins function as RING E3 ligases and negatively regulate plant drought stress-responsive gene expression[J]. The Plant cell, 2008,20(6):1693-1707. doi: 10.1105/tpc.107.057380 URL pmid: 18552202
[88]	Park J-A, Cho SK, Kim JE, et al. Isolation of cDNAs differentially expressed in response to drought stress and characterization of the Ca-LEAL1 gene encoding a new family of atypical LEA-like protein homologue in hot pepper(Capsicum annuum L. cv. Pukang)[J]. Plant science, 2003,165(3):471-481. doi: 10.1016/S0168-9452(03)00165-1 URL
[89]	Lee H K, Cho S K, Son O, et al. Drought stress-induced Rma1H1, a RING membrane-anchor E3 ubiquitin ligase homolog, regulates aquaporin levels via ubiquitination in transgenic Arabidopsis plants[J]. The Plant cell, 2009,21(2):622-641. doi: 10.1105/tpc.108.061994 URL pmid: 19234086
[90]	Ning Y, Jantasuriyarat C, Zhao Q, et al. The SINA E3 ligase OsDIS1 negatively regulates drought response in rice[J]. Plant physiology, 2011,157(1):242-255. doi: 10.1104/pp.111.180893 URL
[91]	Cho S K, Ryu M Y, Song C, et al. Arabidopsis PUB22 and PUB23 are homologous U-Box E3 ubiquitin ligases that play combinatory roles in response to drought stress[J]. Plant Cell, 2008,20(7):1899-1914. doi: 10.1105/tpc.108.060699 URL pmid: 18664614
[92]	Adler G, Konrad Z, Zamir L, et al. The Arabidopsis paralogs, PUB46 and PUB48, encoding U-box E3 ubiquitin ligases, are essential for plant response to drought stress[J]. BMC Plant Biology, 2017,17(8):1-12. doi: 10.1186/s12870-016-0951-9 URL
[93]	方慧敏. 两个E3泛素连接酶基因在水稻耐非生物逆境胁迫中的作用研究[D]. 南京:南京农业大学, 2014.
[94]	唐勋. 马铃薯泛素化蛋白质组学分析及StPUB27基因功能研究[D]. 甘肃:甘肃农业大学, 2018.
[95]	Dong C H, Agarwal M, Zhang Y, et al. The negative regulator of plant cold responses, HOS1, is a RING E3 ligasethat mediates the ubiquitination and degradation of ICE1[J]. Proceedings of the National Academy of Sciences of the United States of America, 2006,103(21):8281-8286. doi: 10.1073/pnas.0602874103 URL pmid: 16702557
[96]	Chinnusamy V. ICE1: a regulator of cold-induced transcriptome and freezing tolerance in Arabidopsis[J]. Genes & development, 2003,17(8):1043-1054. doi: 10.1101/gad.1077503 URL pmid: 12672693
[97]	Lim S D, Cho H Y, Park Y C, et al. The rice RING finger E3 ligase, OsHCI1, drives nuclear export of multiple substrate proteins and its heterogeneous overexpression enhances acquired thermotolerance[J]. Journal of experimental botany, 2013,64(10):2899-2914. doi: 10.1093/jxb/ert143 URL pmid: 23698632
[98]	缴莉. 山葡萄U-box蛋白基因VaPUB的克隆和功能研究[D]. 北京:中国农业大学, 2017.
[99]	李龙. 拟南芥E3泛素连接酶PUB30与PUB31耐盐功能分析及互作的14-3-3蛋白的筛选[D]. 沈阳:沈阳农业大学, 2016.
[100]	Bergler J, Hoth S. Plant U-box armadillo repeat proteins AtPUB18 and AtPUB19 are involved in salt inhibition of germination in Arabidopsis[J]. Plant biology(Stuttgart, Germany), 2011,13(5):725-730.
[101]	Ko J H, Yang S H, Han K H. Upregulation of an Arabidopsis RING-H2 gene, XERICO, confers drought tolerance through increased abscisic acid biosynjournal[J]. The Plant Journal: for cell and molecular biology, 2006,47(3):343-355. doi: 10.1111/tpj.2006.47.issue-3 URL
[102]	Kang M, Fokar M, Abdelmageed H, et al. Arabidopsis SAP5 functions as a positive regulator of stress responses and exhibits E3 ubiquitin ligase activity[J]. Plant molecular biology, 2011,75(4/5):451-466. doi: 10.1007/s11103-011-9748-2 URL
[103]	Miller AJ, Fan X, Orsel M, et al. Nitrate transport and signaling[J]. Journal of Experimental Botany, 2007,58(9):2297-2306. doi: 10.1093/jxb/erm066 URL pmid: 17519352
[104]	Peng M, Hannam C, Gu H, et al. A mutation in NLA, which encodes a RING-type ubiquitin ligase, disrupts the adaptability of Arabidopsis to nitrogen limitation[J]. The Plant Journal: for cell and molecular biology, 2007,50(2):320-337. doi: 10.1111/j.1365-313X.2007.03050.x URL
[105]	Sato T, Maekawa S, Yasuda S, et al. CNI1/ATL31, a RING-type ubiquitin ligase that functions in the carbon/nitrogen response for growth phase transition in Arabidopsis seedlings[J]. The Plant Journal: for cell and molecular biology, 2009,60(5):852-864. doi: 10.1111/tpj.2009.60.issue-5 URL
[106]	Stone S L, Williams L A, Farmer L M, et al. KEEP ON GOING, a RING E3 ligase essential for Arabidopsis growth and development, is involved in abscisic acid signaling[J]. The Plant cell, 2006,18(12):3415-3428. doi: 10.1105/tpc.106.046532 URL pmid: 17194765
[107]	Zhang Y, Yang C, Li Y, et al. SDIR1 is a RING finger E3 ligase that positively regulates stress-responsive abscisic acid signaling in Arabidopsis[J]. The Plant cell, 2007,19(6):1912-1929. doi: 10.1105/tpc.106.048488 URL pmid: 17573536
[108]	庄庄. 东乡野生稻SRFP1基因鉴定与分析[D]. 南昌:江西农业大学, 2016.