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Research Article

Role of Poly-Galacturonase Inhibiting Protein in Plant Defense

, , , &
Pages 91-100 | Received 09 Nov 2005, Accepted 30 Nov 2005, Published online: 11 Oct 2008

REFERENCES

  • Abu-Goukh A. A., Labavitch J. M. The in vivo role of ‘Bartlett’ pear fruit polygalacturonase inhibitors. Physiol Plant Pathol. 1983; 23: 123–135, [CSA]
  • Albersheim P., Anderson A. J. Protein from plant cell wall inhibits polygalacturonases secreted by plant pathogens. Proc. Natl. Acad. Sci. USA 1971; 68: 1815–1819, [CSA]
  • Anbar M. Nitric oxide: A synchronizing chemical messenger. Experientia. 1995; 51: 481–490, [CSA], [CROSSREF]
  • Annie B'ezier, Lambert Bernard, Baillieul Fabienne Study of defense-related gene expression in grapevine leaves and berries infected with Botrytis cinerea. European Journal of Plant Pathology. 2002; 108: 111–120, [CSA], [CROSSREF]
  • ten Have Arjen, Mulder Wietse, Visser Jaap, Jan A., van Kan L. The Endopolygalacturonase Gene Bcpg1 Is Required for Full Virulence of Botrytis cinerea. MPMI 1998; 11(10)1009–1016, [CSA]
  • Becraft P. W. Receptor kinase signaling in plant development. Annu. Rev. Cell. Dev. Biol. 2002; 18: 163–192, [CSA], [CROSSREF]
  • Beligni M. V., Lamattina L. Nitric oxide stimulates seed germinationand de-etiolation, and inhibits hypocotyl elongation, three lightinducible responses in plants. Planta 2000; 210: 215–221, [CSA], [CROSSREF]
  • Berger D. K., Oelofse D., Arendse M. S., Du Plessis E., Dubery I. A. Bean polygalacturonase inhibitor protein-1(PGIP-1) inhibits polygalacturonases from Stenocarpella maydis. Physiological and Molecular Plant Pathology 2000; 57: 5–14, [CSA], [CROSSREF]
  • Bergey D. R., Orozco-Cardenas M., De Moura D. S., Ryan C. A. A wound- and systemin-inducible polygalacturonase in tomato leaves. Proceedings of the National Academy of Sciences of the United States of America 1999; 96: 1756–1760, [CSA], [CROSSREF]
  • Bergmann C. W., Ito Y., Singer D., Albersheim P., Darvill A. G., Benhamou N., Nuss L., Salvi G., Cervone F., De Lorenzo G. Polygalacturonase-inhibiting protein accumulates in Phaseolus vulgaris L. in response to wounding, elicitors and fungal infection. Plant J. 1994; 5(5)625–634, [CSA], [CROSSREF]
  • Bradford M. M. A rapid and sensitive method for the quanti-tation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976; 72: 248–254, [CSA], [CROSSREF]
  • Buza N. L., Krinitsyna A. A., Protsenko M. A., Vartapetyan V. V. Role of the polygalacturonidase inhibitor proteinin the ripening of apples and their resistance to Monilia fructigena, a causative agent of fruit rot. Applied Biochemistry and Microbiology 2004; 40(1)89–92, [CSA], [CROSSREF]
  • Aguero Cecilia, Dandekar Abhaya, Meredith Carole. Evaluation of tolerance to pierce's disease and botrytis in transgenic plants of Vitis vinifera L. expressing the pear pgip gene. ASEV 54th Annual Meeting Reno, Nevada, 2003
  • Cervone F., De Lorenzo G., Pressey R., Darvill A. G., Albersheim P. Can phaseolus PGIP inhibit pectic enzymes from microbes and plants?. Phytochemistry 1990; 29: 447–449, [CSA], [CROSSREF]
  • Cervone F., De Lorenzo G., Degra L., Salvi G., Bergami M. Purification and characterization of polygalacturonase-inhibiting protein from Phaseolus vulgaris L. Plant Physiol. 1987; 85: 631–637, [CSA]
  • Chase M. W., Soltis D. E., Olmstead R. G., Morgan D., Les D. H., Mishler B. D., Duvall M. R., Price R. A., Hills H. G., Qiu Y. L., others. Phylogenetics of seed plants an analysis of nucleotide sequences from the plastid gene RbcL. Annals of the Missouri Botanical Garden 1993; 80: 528–580, [CSA], [CROSSREF]
  • Cook B. J., Clay R. P., Bergmann C. W., Albersheim P., Darvill A. G. Fungal polygalacturonases exhibit different substrate degradation patterns and differ in their susceptibilities to polygalacturonase-inhibiting proteins. Mol. Plant-Microbe Interact. 1999; 12: 703–711, [CSA]
  • De Lorenzo G. Differential accumulation of polygalacturonaseinhibiting (PGIP) mRNA in two near-isogenic lines of Phaseolus vulgaris L. upon infection with Colletotrichum lindemuthianum. Physiol Mol Plant Pathol. 1996; 48: 83–89, [CSA], [CROSSREF]
  • De Lorenzo G., Ferrari S. Polygalacturonase-inhibiting proteins in defense against phytopathogenic fungi. Current Opinion in Plant Biology. 2002; 5: 295–299, [CSA], [CROSSREF]
  • De Lorenzo G., Cervone F., Bellincampi D., Caprari C., Clark A. J., Desiderio A., Devoto A., Forrest R., Leckie F., Nuss L, Salvi G. Polygalacturonase, PGIP and oligogalacturonides in cell–cell communication. Biochemical Society Transactions 1994; 22: 396–399, [CSA]
  • Delledonne M., Xia Y., Dixon R. A., Lamb C. Nitric oxide functions as a signal in plant disease resistance. Nature. 1998; 394: 585–588, [PUBMED], [CSA], [CROSSREF]
  • Delledonne M. NO news is good news for plants. Current Opinion in Plant Biology. 2005; 8: 390–396, [CSA], [CROSSREF]
  • Desiderio A., Aracri B., Leckie F., Mattei B., Salvi G., Tigelaar H., Vanroekel J. S.C., Baulcombe D. C., Melchers L. S., Delorenzo G., Cervone F. Polygalacturonase-inhibiting proteins (PGIPS) with diåerent speciÆcities are expressed in Phaseolus vulgaris. Molecular PlantMicrobe Interactions 1997; 10: 852–860, [CSA]
  • Devoto A., Leckie F., Lupotto E., Cervone F., De Lorenzo G. The promoter of a gene encoding a polygalacturonase-inhibiting protein of Phaseolus vulgaris L. is activated by wounding but not by elicitors or pathogen infection. Planta 1998; 205: 165–174, [CSA], [CROSSREF]
  • Di Matteo A., Federici L., Salvi G., Johnson K. A., Savino C., De Lorenzo G., Tsernoglou D., Cervone F. The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense. Proc. Natl. Acad. Sci. U.S.A. 2003; 100(17)10124–10128, [CSA], [CROSSREF]
  • Dingle J., Reid W. W., Solomons G. L. J. Sci. Food Agric. 1953; 4(2)149–155, [CSA]
  • Durner J., Klessing D. F. Nitric oxide as a signal in plants. Curr. Opin. Plant. Biol. 1999; 2: 369–374, [CSA], [CROSSREF]
  • Elad Y., Evensen K. Physiological aspects of resistance to Botrytis cinerea. Phytopathology 1995; 85: 637–643, [CSA]
  • Ellis J., Dodds P., Pryor T. Structure, function and evolution of plant disease resistance genes. Curr. Opin. Plant. Biol. 2000; 3: 278–284, [CSA], [CROSSREF]
  • Favaron F. Gel detection of Allium porrum polygalacturonaseinhibiting protein reveals a high number of isoforms. Physiol. Mol. Plant Pathol. 2001; 58: 239–245, [CSA], [CROSSREF]
  • Favaron F., D'ovidio R., Porceddu E., Alghisi P. Purification and molecular characterization of a soybean polygalacturonase-inhibiting protein. Planta. 1994; 195: 80–87, [CSA], [CROSSREF]
  • Favaron F., Destro T., D'Ovidio R. Transcript Accumulation Of Polygalacturonase Inhibiting Protein (PGIP) Following Pathogen Infections In Soybean. Journal of Plant Pathology 2000; 82(2)103–109, [CSA]
  • Ferrari S., Vairo D., Ausubel F. M., Cervone F., De Lorenzo G. Tandemly Duplicated Arabidopsis Genes That Encode Polygalacturonase-Inhibiting Proteins Are Regulated Coordinately by Different Signal Transduction Pathwaysin Response to Fungal Infection. The Plant Cell 2003; 15: 93–106, [CSA], [CROSSREF]
  • Fielding A. H. Natural inhibitors of fungal polygalacturonases in infected fruit tissues. J. Gen. Microbiol. 1981; 123: 377–381, [CSA]
  • Fisher M. L., Anderson A. J., Albersheim P. Host–pathogen interactions-VI. A single protein efficiently inhibits endopolygalacturonases secreted by Colletotrichum lindemuthianum and Aspergillus niger. Plant Physiol. 1973; 51: 489–491, [CSA]
  • Fraissinet-Tachet L., Reymond-Cotton P., Fe'vre M. Characterization of a multigene family encoding an endopolygalacturonase in Sclerotinia sclerotiorum. Current Genetics 1995; 29: 96–99, [CSA], [CROSSREF]
  • Frediani M, Cremonini R, Salvi G, Caprari C, Desiderio A. Cytological localization of the pgip genes in the embryo suspensor cells of Phaseolus vulgaris L. Theor Appl Genet 1993; 87: 369–373, [CSA], [CROSSREF]
  • Gazendam I., Oelofse D., Berger D. K. High-level expression of apple PGIP1 is not sufficient to protect transgenic potato against Verticillium dahliae. Physiological and Molecular Plant Pathology 2004; 65: 145–155, [CSA], [CROSSREF]
  • Gomathi V., Gnanamanickam S. S. Polygalacturonase-inhibiting proteins in plant defense. Current Science 2004; 87(9)1211–1217, [CSA]
  • Gomez-Gomez L., Bauer Z., Boller T. Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis. Plant Cell. 2001; 13: 1155–1163, [CSA], [CROSSREF]
  • Guo F. Q., Okamoto Mamoru, Nigel Crawford M. Identi. cation of a Plant Nitric Oxide Synthase Gene Involved inHormonal Signaling. Science 2003; 302: 100–103, [CSA], [CROSSREF]
  • Hadfield K. A., Bennett A. B. Polygalacturonases: many genes in search of a function. Plant physiol. 1998; 117: 337–343, [CSA], [CROSSREF]
  • Hahn M. G., Bucheli P., Cervone F., Doares S. H., O'Neill R. A., Darvill R. A., Albersheim P. The role of cell wall constituents in plant-pathogen interactions. Plant-Microbe Interactions, T. Kosuge, E. W. Nester. Molecular and Genetic Perspectives, McGraw Hill, New York 1989; Vol. 3: 131–181
  • Henrik Stotz U., Ann Powell T., Susan Damon E., Greve Carl, Alan Bennett B., John Labavitch M. Molecular Characterization of a Polygalacturonase lnhibitor from Pyrus communis 1. cv Bartlett. Plant Physiol. 1993; 102: 133–138, [CSA], [CROSSREF]
  • Hoffman R. M., Turner J. G. Occurence and specificity of an endopolygalacturonase inhibitor in Pisum sativum. Physiol Plant Pathol 1984; 24: 49–59, [CSA]
  • Hoffman R. M., Turner J. G. Partial purification of proteins from Pea leaflets that inhibit Ascophyta Pisi endopolygalaturonase. Physiol Plant Pathol 1982; 20: 173–187, [CSA]
  • Jacinda James T., Ian Dubery A. Inhibition of polygalacturonase from Verticillium dahliae by a polygalacturonase inhibiting protein from cotton. Phytochemistry 2001; 57: 149–156, [CSA], [CROSSREF]
  • Johnston D. J., Williamson B., McMillan G. P. The interactionin planta of polygalacturonases from Botrytis cinerea with a cell wall-bound polygalacturonase-inhibiting protein (PGIP) in raspberry fruits. J. Exp. Bot. 1994; 45: 1837–1843, [CSA]
  • Johnston D. J., Ramanathan V., Williamson B. A protein from immature raspberry fruits which inhibits endopolygalacturonases from Botrytis cinerea and other micro-organisms. J. Exp. Bot. 1993; 44: 971–976, [CSA]
  • Jones D. A., Jones J. D.G. The role of leucine-rich repeat proteins in plant defense. Adv Bot Res. 1997; 24: 89–166, [CSA]
  • Jones J. D. Putting knowledge of plant disease resistance genes to work. Curr. Opin. Plant. Biol. 2001; 4: 281–287, [CSA], [CROSSREF]
  • Jones T. M., Anderson A. J., Albersheim P. Host-pathogen interactions. IV. Studies on the polysaccharide-degrading enzymes secreted by Fusarium oxysporum f. Sp. lycopersici. Physiol. Plant Pathol. 1972; 2: 153–166, [CSA]
  • Karr A. L.L., Albersheim P. Polysacride-degrading enzymes are unable to attack plant cell walls without prior action by a “wall-modifying enzymes”. Plant Physicl. 1970; 46: 69–80, [CSA]
  • Kemp G., Bergmann C. W., Clay R., Van der Westhuizen A. J., Pretorius Z. A. Isolation of polygalacturonase–inhibitingprotein (PGIP) from wheat. Mol. Plant–Microb. Interact. 2003; 16: 955–961, [CSA]
  • Kemp G., Stanton L., Bergmann C. W., Clay R. P., Albersheim P., Darvill A. Polygalacturonase-Inhibiting Proteins Can Function as Activators of Polygalacturonase. MPMI 2004; 17(8)888–894, [CSA]
  • Kenneth A., Shackel, Maria de la Paz Celorio-Mancera, Ahmadi Hamid, Carl Greve L., Larry Teuber R., Elaine Backus A., John Labavitchl M. Micro-Injection of Lygus Salivary Gland Proteins to Simulate Feeding Damage in Alfalfa and Cotton Flowers. Archives of Insect Biochemistry and Physiology. 2005; 58: 69–83, [CSA], [CROSSREF]
  • Kistner C., Parniske M. Evolution of signal transduction in intracellular symbiosis. Trends Plant Sci. 2002; 7: 511–518, [CSA], [CROSSREF]
  • Kobe B., Kajava A. V. The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol. 2001; 11: 725–732, [CSA], [CROSSREF]
  • Lafitte C., Barthe J. B., Montillet J. L., Touze A. Glycoprotein inhibitors of Colletotrichum lindemuthianum endopoygalacturonase in near isogenic lines of Phaseolus vulgaris resistant and susceptible to anthracnose. Physiol Plant Pathol. 1984; 25: 39–53, [CSA]
  • Lamb C. A Ligand-Receptor Mechanism in Plant-Pathogen Recognition. Science 1996; 274: 2038–2039, [CSA], [CROSSREF]
  • Lang C., Dornenburg H. Perspectives in the biological function and the technological application of polygalacturonases. Applied Microbiology and Biotechnology 2000; 53: 366–375, [CSA], [CROSSREF]
  • Leech A., Mattei B., Federici B., De Lorenzo G., Hemmings A. M. Preliminary X-ray crystallographic analysis of a plant defense protein, the polygalacturonase-inhibiting protein from Phaseolus vulgaris. Acta Cryst. 2002; 56: 98–100, [CSA]
  • Leshem Y. Y., Wills R. B.H., Ku V. V. Evidence for the function of the free radical gas-nitric oxide. NO. as an endogenous maturation and senescence regulating factor in higher plants. Plant Physiol. Biochem. 1998; 36: 825–833, [CSA], [CROSSREF]
  • Liang F. S., Zhang K. C.H., Zhou Ch. J., Kong F. N., Lia J., Wang B. Cloning, characterization and expression of the gene encoding polygalacturonase-inhibiting proteins (PGIPs) of peach [prunus persica (L.) Batch]. Plant Science 2005; 168: 481–486, [CSA], [CROSSREF]
  • Mehli Lisbeth, Jan Schaart G., Trygve Kjellsen D., Hong Tran Diem, Elma M., Salentijn J., Henk Schouten J., Tor-Henning Iversen. A gene encoding a polygalacturonase-inhibiting protein(PGIP) shows developmental regulation and pathogen-induced expression in strawberry. New Phytologist. 2004; 163: 99–110, [CSA], [CROSSREF]
  • Mehli Lisbeth, Trygve Kjellsen D., Frances Dewey M., Ari Hietala M. A case study from the interaction of strawberry and Botrytis cinerea highlights the benefits of comonitoring both partners at genomic and mRNA level. New Phytologist 2005; 10: 1469–8137, 1111/j[CSA]
  • Martin G. B., Bogdanove A. J., Sessa G. Understanding the functions of plant disease resistance proteins. Annu Rev Plant Biol. 2003; 54: 23–61, [CSA], [CROSSREF]
  • Mata C. G., Lamattina L. Nitric oxide induces stomatal closure and enhances the adaptive plant responses against drought stress. Plant Physiol. 2001; 126: 1196–1204, [CSA], [CROSSREF]
  • Mattei B., Galletti R., Manfredini C., Pontiggia D., Salvi G., Spadoni S., Caprari C., Ferrari S., Bellincampi D., Cervone F., De Lorenzo G. Recognition and signalling in the cell wall: The case of endopolygalacturonase, PGIP and oligogalacturonides. Plant Biosystems. 2005; 139: 24–27, [CSA]
  • Milagros Machinandiarena F., Florencia Olivieri P., Gustavo Daleo R., Claudia Oliva R. Isolation and characterization of a polygalacturonase-inhibiting protein from potato leaves. Accumulation in response to salicylic acid, wounding and infection. Plant Physiol. Biochem. 2001; 39: 129–136, [CSA], [CROSSREF]
  • Nuss L., Mahé A., Clark A. J., Grisvard J., Dron M., Cervone F., Walton J. D. Deconstructing the cell wall. Plant Physiology 1994; 104: 113–118, [CSA]
  • Pedroso M. C., Durzan D. J. Effects of different gravity environments on DNA fragmentation and cell death in Kalanchoe leaves. Ann. Bot. 2000; 86: 983–994, [CSA], [CROSSREF]
  • Powell A. L.T., van Kan J., ten Have A., Visser J., Greve L. C., Bennett A. B., Labavitch J. M. Transgenic expression of pear PGIP in tomato limits fungal colonization. Mol. Plant Microbe Interact. 2000; 13: 942–950, [CSA]
  • Powell A. L.T., Stotz H. U., Labavitch J. M., Bennett A. B. Glycoprotein inhibitors of fungal polygalacturonases. Advances in Molecular Genetics of Plant-Microbe Interactions, M. J. Daniels, J. A. Downie, A. E. Osbourn. Kluwer Academic Pub., DordrechtThe Netherlands 1994; 399–402, protein from apple fruit. Phytopathology 85 1373-1377
  • D'Ovidio Renato, Raiola Alessandro, Capodicasa Cristina, Alessandra Devoto, Pontiggia Daniela, Roberti Serena, Galletti Roberta, Conti Eric, O'Sullivan Donal, De Lorenzo Giulia. Characterization of the Complex Locus of Bean Encoding Polygalacturonase-Inhibiting Proteins Reveals Subfunctionalization for Defense against Fungi and Insects. Plant Physiology. 2004; 135: 2424–2435, [CSA], [CROSSREF]
  • D'Ovidio Renato, Benedetta Mattei, Roberti Serena, Bellincampi Daniela. Polygalacturonases, polygalacturonase-inhibiting proteins and pectic oligomers in plant–pathogen interactions. Biochimica et Biophysica Acta. 2004; 1696: 237–244, [CSA]
  • Rugang L i, Rimmer Roger, Min Yu, Andrew Sharpe G., Se'guin-Swartz Ginette, Lydiate Derek, Dwayne Hegedus D. Two Brassica napuspolygalacturonase inhibitory protein genes are expressed at different levels in response to biotic and abiotic stresses. Planta. 2003; 217: 299–308, [CSA]
  • Salvi G., Giarrizzo F., De Lorenzo G., Cervone F. A polygalacturonase-inhibiting protein in the flowers Phaseolus vulgaris L. J. Plant Physiol. 1990; 136: 513–518, [CSA]
  • Shanmugam V. Role of extracytoplasmic leucine rich repeat proteins in plant defense mechanisms. Microbiological Research. 2005; 160: 83–94, [CSA], [CROSSREF]
  • Sharrock K. R., Labavitch J. M. Polygalacturonase inhibitors of Bartlett pear fruits: differential effects on Botrytis cinerea polygalacturonase isozymes, and influence on products of fungal hydrolysis of pear cell walls and on ethylene induction in cell culture. Physiol. Mol. Plant Pathol. 1994; 45: 305–319, [CSA], [CROSSREF]
  • Shieh M. T., Brown R. L., Whitehead M. P., Cary J. W., Cotty P. J., Cleveland T. E., Dean R. A. Molecular genetic evidence for the involvement of a specific polygalacturonase, P, in the invasion and spread of Aspergillus flavus in cotton bolls. Appl Environ Microbiol. 1997; 63: 3548–3552, [CSA]
  • Staskawicz B. J., Ausubel F. M., Ellis J. G., Jones J. D.G. A Ligand-Receptor Mechanism in Plant-Pathogen Recognition. Science 1995; 268: 661, [CSA]
  • Stotz H. U., Contos J. J., Powell A. L., Bennett A. B., Labavitch J. M. Structure and expression of an inhibitor of fungal polygalacturonases from tomato. Plant Mol Biol. 1994; 25(4)607–617, [CSA], [CROSSREF]
  • Sudha G., Ravishankar G. A. Involvement and interaction of various signaling compounds on the plant metabolic events during defense response, resistance to stress factors, formation of secondary metabolites and their molecular aspects. Plant Cell, Tissue and Organ Culture. 2002; 71: 181–212, [CSA], [CROSSREF]
  • Szankowski I., Briviba K., Fleschhut J., Schnherr J., Jacobsen H. -J., Kiesecker H. Transformation of apple (Malus domestica Borkh.) with the stilbene synthase gene from grapevine (Vitis vinifera L.) and a PGIP gene from kiwi (Actinidia deliciosa). Plant Cell Rep. 2003; 22: 141–149, [CSA], [CROSSREF]
  • Szekeres M. Brassinosteroid and systemin: Two hormones perceived by the same receptor. Trends Plant Sci. 2003; 8: 102–104, [CSA], [CROSSREF]
  • Tamura M., Gao M., Tao R., Labavitch J. M., Dandekar A. M. Transformation of persimmon with a pear fruit polygalacturonase inhibiting protein (PGIP) gene. Scientia Horticulturae. 2004; 103: 19–30, [CSA], [CROSSREF]
  • Taylor R. J., Secor G. A. An improved diffusion assay for quantifying the polygalacturonase content of Envinia culture filtrates. Phytopathology. 1988; 78: 1101–1103, [CSA]
  • Toubart P., Desiderio A., Salvi G., Cervone F., Daroda L., De Lorenzo G., Bergmann C., Darvill A. G., Albersheim P. Cloning and characterization of the gene encoding the endopolygalacturonase-inhibiting protein (PGIP) of Phaseolus vulgaris. L. Plant J. 1992; 2: 367–373, [CSA]
  • Turner J. G., Hoffman R. M. Effect of the PGIP from Pea on the hydrolysis of Pea cell walls by the endo-PG from Ascochyta pisi. Plant Pathol. 1985; 34: 54–60, [CSA]
  • Wayne W. Fish. Polygalacturonase-inhibiting protein activity in cantaloupe fruit as a function of fruit maturation and tissue origin. European Journal of Plant Pathology 2005; 111: 67–76, [CSA], [CROSSREF]
  • Xue L., Zhang Y., Zhang T., An L., Wang X. Effects of Enhanced Ultraviolet-B Radiation on Algae and Cyanobacteria. Critical Reviews in Microbiology 2005; 31: 79–89, [CSA], [CROSSREF]
  • Yakoby N., Kobiler I., Dinoor A., Prusky D. pH regulation of pectate lyase secretion modulates the attack of Colletotrichum gloeosporioides on avocado fruits. App. Environ. Microbiol. 2000; 66: 1026–1030, [CSA], [CROSSREF]
  • Yao C., Conway W. S., Saams C. E. Purification and characterization of a polygalacturonase inhibiting protein from apple fruit. Phytopathology. 1995; 85: 1373–1377, [CSA]
  • Yao C. L., Conway W. S., Ren R. H., Smith D., Ross G. S., Sams C. E. Gene encoding polygalacturonase inhibitor in apple fruit is developmentally regulated and activated by wounding and fungal infection. Plant Molecular Biology. 1999; 39: 1231–1241, [CSA], [CROSSREF]
  • Yu-Ying H., Klisch M., Haeder D. -P. Adaptation of cyanobacteria to UV-B stress correlated with oxidative stress and oxidative damage. Photochemistry and Photobiology 2002; 76(2)188–196, [CSA], [CROSSREF]
  • Zhang M., Lizhe A., Feng H., et al. The cascade mechanisms of nitric oxide as a second messenger of ultravioletBin inhibiting mesocotyl elongations. Photochemistry and Photobiology 2003; 77: 219–225, [CSA], [CROSSREF]
  • Zhao L., Zhang F., Yang J., Li B., Zhang L. Nitric oxide functions as a signal salt resistance in the calluses from two ecotypes of Reed. Plant Physiol. 2004; 134: 849–857, [CSA], [CROSSREF]

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