植物天冬氨酸蛋白酶的研究进展

doi:10.13560/j.cnki.biotech.bull.1985.2016.01.003

摘要/Abstract

摘要： 天冬氨酸蛋白酶是四大类蛋白水解酶之一, 广泛存在于多种生物中, 参与了很多重要的生理过程。相对于其他生物而言, 对植物天冬氨酸蛋白酶的研究相对滞后。自20世纪末以来, 这一领域的工作取得了重大进展。经典的植物天冬氨酸蛋白酶除了具有保守的蛋白酶结构域外还有一段植物特有的插入片段;在动植物分离之后, 植物天冬氨酸蛋白酶基因家族进行了大规模的扩增;该类蛋白酶在植物的整个生长发育过程中发挥重要的功能, 尤其是胁迫反应、有性生殖、衰老和程序性死亡以及蛋白质的加工和降解。对近些年植物天冬氨酸蛋白酶的研究进展进行综述, 并对其未来的发展进行展望。

关键词: 天冬氨酸蛋白酶, 加工和灭活机制, 胁迫反应, 有性生殖, 程序性死亡

Abstract: Aspartic proteinases constitute one of four super-families of proteolytic enzymes, and are widely distributed in varied living organisms and involved in many biological processes. Compared with other organisms, the research on plant aspartic proteinases is relatively lagging behind. Since the end of last century, significant progress has been made in this area. Except conserved proteinase domain, typical plant aspartic proteinases have a specific insert only in plant. After the separation of plant and animal, the gene family of aspartic proteinases has expanded largely;these proteinases play important role in whole progress of plant growth and development, especially in stress response, sexual reproduction, senescence and programmed cell death, and the processing and degradation of protein. In this context, the research advances in plant aspartic protease is reviewed and its future development is prospected.

Key words: aspartic proteinase, processing and inactivation mechanism, stress response, sexual reproduction, programmed cell death

葛伟娜, 李超, 张家琦, 张岚, 王振怡. 植物天冬氨酸蛋白酶的研究进展[J]. 生物技术通报, 2016, 32(1): 8-14.

GE Wei-na, LI Chao, ZHANG Jia-qi, ZHANG Lan, WANG Zhen-yi. Research Advances on Plant Aspartic Proteinase[J]. Biotechnology Bulletin, 2016, 32(1): 8-14.

参考文献

［1］ Simoes I, Faro C. Structure and function of plant aspartic proteinas-es［J］. Eur J Biochem, 2004, 271(11)：2067-2075.
［2］ Rawlings ND, Waller M, Barrett AJ, et al. MEROPS：the database of proteolytic enzymes, their substrates and inhibitors［J］. Nucleic Acids Res, 2014, 42(Database issue)：D503-509.
［3］ Lufrano D, Faro R, Castanheira P, et al. Molecular cloning and characterization of procirsin, an active aspartic protease precursor from Cirsium vulgare(Asteraceae)［J］. Phytochemistry, 2012, 81：7-18.
［4］ Gonzalez-Rabade N, Badillo-Corona JA, Aranda-Barradas JS, et al. Production of plant proteases in vivo and in vitro—a review［J］. Biotechnology Advances, 2011, 29(6)：983-996.
［5］ Rocha GF, Obregon WD, Munoz F, et al. Isolation and characteriza-tion of an aspartic protease from Salpichroa origanifolia fruits［J］. Protein and Peptide Letters, 2015, 22(4)：379-390.
［6］ Yin C, Zheng L, Chen L, et al. Cloning, expression, and characteriza-tion of a milk-clotting aspartic protease gene(Po-Asp)from Pleu-rotus ostreatus［J］. Applied Biochemistry and Biotechnology, 2014, 172(4)：2119-2131.
［7］ Faro C, Gal S. Aspartic proteinase content of the Arabidopsis genome［J］. Curr Protein Pept Sci, 2005, 6(6)：493-500.
［8］ Chen F, Foolad MR. Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration［J］. Plant Molecular Biology, 1997, 35：821-831.
［9］ Nakano T, Murakami S, Shoji T, et al. A Nove1 protein with DNA binding activity from tobacco chloroplast nucleoids［J］. The Plant Cell, 1997, 9：1673-1682.
［10］ Xia Y, Suzuki H, Borevitz J, et al. An extracellular aspartic protease functions in Arabidopsis disease resistance signaling［J］. EMBO J, 2004, 23(4)：980-988.
［11］ Prasad BD, Creissen G, Lamb C, et al. Overexpression of rice(Oryza sativa L.)OsCDR1 leads to constitutive activation of defense responses in rice and Arabidopsis［J］. Mol Plant Microbe Interact, 2009, 22(12)：1635-1644.
［12］ Frazao C, Bento I, Costa J, et al. Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L. ［J］. J Biol Chem, 1999, 274(39)：27694-27701.
［13］ Kervinen J, Tobin GJ, Costa J, et al. Crystal structure of plant aspartic proteinase prophytepsin：inactivation and vacuolar targeting［J］. EMBO J, 1999, 18(14)：3947-3955.
［14］ Vairo Cavalli S, Lufrano D, Colombo ML, et al. Properties and applications of phytepsins from thistle flowers［J］. Phytochemistry, 2013, 92：16-32.
［15］ Bryksa BC, Bhaumik P, Magracheva E, et al. Structure and mechanism of the saposin-like domain of a plant aspartic protease［J］. J Biol Chem, 2011, 286(32)：28265-28275.
［16］ Anderson DH, Sawaya MR, Cascio D, et al. Granulysin crystal structure and a structure-derived lytic mechanism［J］. J Mol Biol, 2003, 325(2)：355-365.
［17］ De Moura DC, Bryksa BC, Yada RY. In silico insights into protein-protein interactions and folding dynamics of the saposin-like domain of Solanum tuberosum aspartic protease［J］. PLoS One, 2014, 9(9)：e104315.
［18］ Tormakangas K, Hadlington JL, Pimpl P, et al. A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum［J］. Plant Cell, 2001, 13(9)：2021-2032.
［19］ Munoz FF, Mendieta JR, Pagano MR, et al. The swaposin-like domain of potato aspartic protease(StAsp-PSI)exerts antimicrobial activity on plant and human pathogens［J］. Peptides, 2010, 31(5)：777-785.
［20］ Munoz F, Palomares-Jerez MF, Daleo G, et al. Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes［J］. Biochimica et Biophysica Acta, 2014, 1838(1 Pt B)：339-347.
［21］ Schaller A, Ryan CA. Molecular cloning of a tomato leaf cDNA encoding an aspartic protease, a systemic wound response protein［J］. Plant Mol Biol, 1996, 31(5)：1073-1077.
［22］ An CI, Fukusaki E, Kobayashi A. Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco［J］. Planta, 2002, 214(5)：661-667.
［23］ Curto P, Lufrano D, Pinto C, et al. Establishing the yeast Kluyveromyces lactis as an expression host for production of the saposin-like domain of the aspartic protease cirsin［J］. Applied and Environmental Microbiology, 2014, 80(1)：86-96.
［24］ Terauchi K, Asakura T, Ueda H, et al. Plant-specific insertions in the soybean aspartic proteinases, soyAP1 and soyAP2, perform different functions of vacuolar targeting［J］. J Plant Physiol, 2006, 163(8)：856-862.
［25］ Ramalho-Santos M, Verissimo P, Cortes L, et al. Identification and proteolytic processing of procardosin A［J］. Eur J Biochem, 1998, 255(1)：133-138.
［26］ Glathe S, Kervinen J, Nimtz M, et al. Transport and activation of the vacuolar aspartic proteinase phytepsin in barley(Hordeum vulgare L.)［J］. J Biol Chem, 1998, 273(47)：31230-31236.
［27］ White PC, Cordeiro MC, Arnold D, et al. Processing, activity, and inhibition of recombinant cyprosin, an aspartic proteinase from cardoon(Cynara cardunculus)［J］. J Biol Chem, 1999, 274(24)：16685-16693.
［28］ Richter C, Tanaka T, Yada RY. Mechanism of activation of the gastric aspartic proteinases：pepsinogen, progastricsin and prochymosin［J］. Biochem J, 1998, 335(Pt 3)：481-490.
［29］ Takahashi K, Niwa H, Yokota N, et al. Widespread tissue expression of nepenthesin-like aspartic protease genes in Arabidopsis thaliana ［J］. Plant Physiol Biochem, 2008, 46(7)：724-729.
［30］ Chen J, Ouyang Y, Wang L, et al. Aspartic proteases gene family in rice：Gene structure and expression, predicted protein features and phylogenetic relation［J］. Gene, 2009, 442(1-2)：108-118.
［31］ Guo R, Xu X, Carole B, et al. Genome-wide identification, evolutionary and expression analysis of the aspartic protease gene superfamily in grape［J］. BMC Genomics, 2013, 14：554.
［32］ Dunn BM. Structure and mechanism of the pepsin-like family of aspartic peptidases［J］. Chem Rev, 2002, 102(12)：4431-4458.
［33］ Geier G, Banaj HJ, Heid H, et al. Aspartyl proteases in Caenorhab-ditis elegans. Isolation, identification and characterization by a com- bined use of affinity chromatography, two-dimensional gel electrop-horesis, microsequencing and databank analysis［J］. Eur J Bio-chem, 1999, 264(3)：872-979.
［34］ Breitenbach HH, Wenig M, Wittek F, et al. Contrasting roles of the apoplastic aspartyl protease APOPLASTIC, ENHANCED DISEASE SUSCEPTIBILITY1-DEPENDENT1 and LEGUME LECTIN-LIKE PROTEIN1 in Arabidopsis systemic acquired resistance［J］. Plant Physiology, 2014, 165(2)：791-809.
［35］ Mendieta JR, Pagano MR, Munoz FF, et al. Antimicrobial activity of potato aspartic proteases(StAPs)involves membrane permeabilization［J］. Microbiology, 2006, 152(Pt 7)：2039-2047.
［36］ Mendieta JR, Fimognari C, Daleo GR, et al. Cytotoxic effect of potato aspartic proteases(StAPs)on Jurkat T cells［J］. Fitoterapia, 2010, 81(5)：329-335.
［37］ Yao X, Xiong W, Ye T, et al. Overexpression of the aspartic protease ASPG1 gene confers drought avoidance in Arabidopsis［J］. J Exp Bot, 2012, 63(7)：2579-2593.
［38］ Contour-Ansel D, Torres-Franklin ML, Zuily-Fodil Y, et al. An aspartic acid protease from common bean is expressed ‘on call’ during water stress and early recovery［J］. J Plant Physiol, 2010, 167(18)：1606-1612.
［39］ Raimbault AK, Zuily-Fodil Y, Soler A, et al. A novel aspartic acid protease gene from pineapple fruit(Ananas comosus)：cloning, characterization and relation to postharvest chilling stress resistance［J］. J Plant Physiol, 2013, 170(17)：1536-1540.
［40］ Timotijevic GS, Milisavljevic M, Radovic SR, et al. Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat ［J］. J Plant Physiol, 2009, 167(1)：61-68.
［41］ Huang J, Zhao X, Cheng K, et al. OsAP65, a rice aspartic protease, is essential for male fertility and plays a role in pollen germination and pollen tube growth［J］. J Exp Bot, 2013, 64(11)：3351-3360.
［42］葛伟娜. 拟南芥花粉萌发过程中质外体蛋白质组学的研究［D］. 石家庄：河北师范大学, 2011.
［43］ Kato Y, Murakami S, Yamamoto Y, et al. The DNA-binding protease, CND41, and the degradation of ribulose-1, 5-bisphosphate carboxylase/oxygenase in senescent leaves of tobacco［J］. Planta, 2004, 220(1)：97-104.
［44］ Ge X, Dietrich C, Matsuno M, et al. An Arabidopsis aspartic protease functions as an anti-cell-death component in reproduction and embryogenesis［J］. EMBO Rep, 2005, 6(3)：282-288.
［45］ Breckenridge DG, Germain M, Mathai JP, et al. Regulation of apoptosis by endoplasmic reticulum pathways［J］. Oncogene, 2003, 22(53)：8608-8618.
［46］ Chen J, Ding J, Ouyang Y, et al. A triallelic system of S5 is a major regulator of the reproductive barrier and compatibility of indica-japonica hybrids in rice［J］. Proc Natl Acad Sci USA, 2008, 105(32)：11436-11441.
［47］ Yang J, Zhao X, Cheng K, et al. A killer-protector system regulates both hybrid sterility and segregation distortion in rice［J］. Science, 2012, 337(6100)：1336-1340.
［48］ Hiraiwa N, Kondo M, Nishimura M, et al. An aspartic endopeptidase is involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles of plants［J］. Eur J Biochem, 1997, 246(1)：133-141.
［49］ D’Hondt K, Bosch D, Van Damme J, et al. An aspartic proteinase present in seeds cleaves Arabidopsis 2 S albumin precursors in vitro［J］. J Biol Chem, 1993, 268(28)：20884-20891.
［50］ An CI, Fukusaki E, Kobayashi A. Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco［J］. Planta, 2002, 214(5)：661-667.
［51］ Buch F, Kaman WE, Bikker FJ, et al. Nepenthesin protease activity indicates digestive fluid dynamics in carnivorous nepenthes plants［J］. PLoS One, 2015, 10(3)：e0118853.
［52］ Chaturvedi P, Surve S, Mukherjee S, et al. Aspartic protease gene expression and kaempferol production at different germinating stages of cow pea(Vigna articulata L.)seeds varieties［J］. Euro J Exp Bio, 2013, 3(4)：123-133.
［53］Salvador SM, Novo C, Domingos A. Evaluation of the presence of aspartic proteases from Centaurea calcitrapa during seed germination［J］. Enzyme and Microbial Technology, 2006, 38(7)：893-898.

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[7]	吴晨紫;杨志伟;. 细菌对胁迫应答因子RpoS的调控[J]. , 2010, 0(12): 50-55.
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[9]	敏云馨;马忠仁;. 细胞程序性死亡通路的研究进展[J]. , 2009, 0(11): 20-23.
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[11]	丁宁;沈元月;冯永庆;秦岭;. 植物细胞程序性死亡分子机制和信号转导[J]. , 2008, 0(01): 25-29.
[12]	. 国外动态[J]. , 2003, 0(05): 47-48.
[13]	孙雷心. 普通乳蛋白体外抑制癌症[J]. , 1996, 0(02): 21-22.
[14]	孙国凤;. 来自F_1品种的人工种苗的田间试验成功[J]. , 1989, 0(06): 23-24.