Two cell wall Kunitz trypsin inhibitors in chickpea during seed germination and seedling growth

Plant Physiology and Biochemistry

Volumn 47, Issue 3, 2009, Pages 181-187

  Hernández Nistal, Josefina ^a   Martín, Ignacio ^b   Jiménez, Teresa ^b   Dopico, Berta ^b   Labrador, Emilia ^b  

^a UNIVERSITY OF SANTIAGO DE COMPOSTELA   (Spain)

^b UNIVERSITY OF SALAMANCA   (Spain)

Author keywords

Cell wall; Cicer arietinum; Embryonic axes; Proteinase inhibitor; Seed germination; Vascular tissue

Indexed keywords

KUNITZ TYPE PROTEASE INHIBITOR, PLANT; KUNITZ-TYPE PROTEASE INHIBITOR, PLANT; PEPTIDE; VEGETABLE PROTEIN;

ARTICLE; CELL WALL; CHEMISTRY; CHICKPEA; GERMINATION; GROWTH, DEVELOPMENT AND AGING; IMMUNOHISTOCHEMISTRY; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PLANT SEED; WESTERN BLOTTING;

BLOTTING, WESTERN; CELL WALL; CICER; GERMINATION; IMMUNOHISTOCHEMISTRY; MOLECULAR SEQUENCE DATA; PEPTIDES; PLANT PROTEINS; SEEDS;

CICER ARIETINUM;

EID: 59049086814     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2008.11.009     Document Type: Article

References (40)

1. Abe K., Emori Y., Kondo H., Suzuki K., and Arai S. Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). J. Biol. Chem. 262 (1987) 16793-16797
2. Baumgartmer B., and Chrispeels M.J. Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cotyledons of mung bean. Plant Physiol. 58 (1976) 1-6
3. Downing W.L., Mauxion F., Fauvarque M., Reviron M., de Vienne D., Vartanian N., and Giraudat J. A Brassica napus transcript encoding a protein related to the Kunitz protease inhibitor family accumulates upon water stress in leaves, not in seeds. Plant J. 2 (1992) 685-693
4. Endo S., Demura T., and Fukuda H. Inhibition of proteasome activity by the TED4 protein in extracellular space: a novel mechanism for protection of living cells from injury caused by dying cells. Plant Cell Physiol. 42 (2001) 9-19
5. Groover A., and Jones A.M. Tracheary element differentiation uses a novel mechanism coordinating programmed cell death and secondary cell wall synthesis. Plant Physiol. 119 (1999) 375-384
6. Harlow E., and Lane D. Antibodies: A Laboratory Manual (1988), Cold Spring Harbor Laboratory Press, Plainview, NY
7. Hedeman M., Welham T., Boisen S., Canibe N., Bilham L., and Domoney C. Studies on the biological responses of rats to seed trypsin inhibitors using near-isogenic lines of Pisum sativum L. J. Sci. Food Agr. 79 (1999) 1647-1653
8. Hernández-Nistal J., Labrador E., Martín I., Jiménez T., and Dopico B. Transcriptional profiling of cell wall protein genes in chickpea embryonic axes during germination and growth. Plant Physiol. Biochem. 44 (2006) 684-692
9. Jiménez T., Martín I., Labrador E., and Dopico B. A chickpea Kunitz trypsin inhibitor is located in cell wall of elongating seedling organs and vascular tissue. Planta 226 (2007) 45-55
10. Jiménez T., Martín I., Hernández-Nistal J., Labrador E., and Dopico B. The accumulation of a Kunitz trypsin inhibitor from chickpea (TPI-2) located in cell walls is increased in wounded leaves and elongating epicotyls. Physiol. Plant. 132 (2008) 306-317
11. Jofuku K.D., Schipper R.D., and Goldberg R.B. A frameshift mutation prevents Kunitz trypsin inhibitor mRNA accumulation in soybean embryos. Plant Cell 1 (1989) 427-435
12. Jofuku K.D., and Goldberg R.B. Kunitz trypsin inhibitor genes are differentially expressed during the soybean life cycle and in transformed tobacco plants. Plant Cell 1 (1989) 1079-1093
13. Johnson E.D., Miller E.A., and Anderson M.A. Dual location of a family of proteinase inhibitors within the stigmas of Nicotiana alata. Planta 225 (2007) 1265-1276
14. Kim S., Hong Y., An C.S., and Lee K. Expression characteristic of serin protease inhibitors II under variable environmental stresses in hot pepper (Capsicum annuum L.). Plant Sci. 161 (2001) 27-33
15. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
16. Lingaraju M.H., and Gowda L.R. A Kunitz trypsin inhibitor of Entada scandens seeds: another member with single disulfide bridge. Biochim. Biophys. Acta 1784 (2008) 850-855
17. Macedo M.L.R., García V.A., Freire M.G.M., and Richardson M. Characterization of a Kunitz trypsin inhibitor with a single disulfide bridge from seeds of Inga laurina (SW.) Willd. Phytochemistry 68 (2007) 1104-1111
18. Muñoz F.J., Dopico B., and Labrador E. Two growth-related organ-specific cDNAs from Cicer arietinum epicotyls. Plant Mol. Biol. 35 (1997) 433-442
19. Múzquiz M., Welham T., Altares P., Goyoaga C., Cuadrado C., Romero C., Gullamón E., and Domoney C. The effect of germination on seed trypsin inhibitors in Vicia faba and Cicer arietinum. J. Sci. Food Agric. 84 (2004) 556-560
20. Nakabayashi K., Okamoto M., Koshiba T., Kaniya Y., and Nambara E. Genome-wide profiling of stored mRNA in Arabidopsis thaliana seed germination: epigenetic and genetic regulation of transcription in seeds. Plant J. 41 (2005) 697-709
21. Nambara E., Hayama R., Tsuchiya Y., Nishimura M., Kawaide H., Kamiya Y., and Naito S. The role of ABI3 and FUS3 loci in Arabidopsis thaliana on phase transition from late embryo development to germination. Dev. Biol. 220 (2000) 412-423
22. Parcy F., Valon C., Kohara A., Miséra S., and Giraudat J. The ABSCISIC ACID-INSENSITIVE3, FUSCA3, and LEAFY COTYLEDON1 loci act in concert to control multiple aspects of Arabidopsis seed development. Plant Cell 9 (1997) 1266 1277
23. Poerio E., Carranzo L., Garzillo A.M., and Buonocore V. A trypsin inhibitor from the water-soluble fraction of wheat kernel. Phytochemistry 28 (1989) 1307-1311
24. Pusztai A. Metabolism of trypsin inhibitor proteins in the germinating seeds of kidney bean (Phaseolus vulgaris). Planta 107 (1972) 121-129
25. Richardson M. Seed storage proteins: the enzyme inhibitors. In: Dey P.M., and Harborne J.B. (Eds). Methods in Plant Biochemistry. Amino Acids, Proteins and Nucleic Acids vol. 5 (1991), Academic Press Inc., San Diego 259-305
26. Ryan C.A. Proteolytic enzymes and their inhibitors in plants. Annu. Rev. Plant Physiol. 24 (1973) 173-196
27. Ryan C.A. Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 28 (1990) 425-449
28. Saarikoski P., Clapham D., and Von Arnold S. A wound-inducible gene from Saliz viminalis coding for a trypsin inhibitor. Plant Mol. Biol. 31 (1996) 465-478
29. Sin S.-F., Yeung E.C., and Chye M.L. Downregulation of Solanum americanum genes encoding proteinase inhibitor II causes defective seed development. Plant J. 46 (2006) 58-70
30. Spencer M.E., and Hodge R. Cloning and sequencing of the cDNA encoding the major albumin of Theobroma cacao. Identification of the protein as a member of the Kunitz protease inhibitor family. Planta 183 (1991) 528-535
31. Stotz H.U., Kroymann J., and Mitchell O. Plant-insect interactions. Curr. Opin. Plant Biol. 2 (1999) 268-272
32. Tamayo M.C., Rufat M., Bravo J.M., and San Segundo B. Accumulation of a maize proteinase inhibitor in response to wounding and insect feeding, and characterization of its activity toward digestive proteinase of Spodoptera littoralis larvae. Planta 211 (2000) 62-71
33. Welham T., and Domoney C. Temporal and spatial activity of a promoter from a pea enzyme inhibitor gene and its exploitation for seed quality improvement. Plant Sci. 159 (2000) 289-299
34. Welham T., O'Neill M., Johnson S., Wang T.L., and Domoney C. Expression patterns of genes encoding seed trypsin inhibitors in Pisum sativum. Plant Sci. 131 (1998) 13-24
35. Wilson K.A. The proteolysis of trypsin inhibitors in legume seeds. Crit. Rev. Biotechnol. 8 (1988) 197-216
36. Wilson K.A. The protease inhibitors of seeds. In: Larkins B.A., and Vasil I.K. (Eds). Cellular and Molecular Biology of Plant Seed Development (1997), Kluwer Academic Publishing, Dordrecht 331-374
37. Worthington C.C. Worthington Manual, Enzymes and Related Biochemicals (1988), Worthington Biochemical Corporation, Freehold, NJ
38. Yeh K.W., Chen J.C., Lin M.I., Chen Y.M., and Lin C.Y. Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity. Plant Mol. Biol. 33 (1997) 565-570
39. Zavala J.A., Patankar A.G., Gase K., Hui D., and Baldwin I.T. Manipulation of endogenous trypsin proteinase inhibitor production in Nicotiana attenuata demonstrates their function as antiherbivore defenses. Plant Physiol. 134 (2004) 1181-1190
40. Zhang H., Xie X., Xu Y., and Wu N. Isolation and functional assessment of a tomato proteinase inhibitor II gene. Plant Physiol. Biochem. 42 (2004) 437-444