Induction of leucine aminopeptidase (LAP) like activity with wounding and methyl jasmonate in pigeonpea (Cajanas cajan) suggests the role of these enzymes in plant defense in leguminosae

Plant Physiology and Biochemistry

Volumn 49, Issue 6, 2011, Pages 609-616

  Lomate, Purushottam R ^a   Hivrale, Vandana K ^a  

^a DR BABASAHEB AMBEDKAR MARATHWADA UNIVERSITY   (India)

Author keywords

Aminopeptidases; Induction; Methyl jasmonate; Pigeonpea; Plant defense; Wounding

Indexed keywords

ACETIC ACID DERIVATIVE; CYCLOPENTANE DERIVATIVE; CYTOSOL AMINOPEPTIDASE; ENZYME INHIBITOR; JASMONIC ACID METHYL ESTER; MAGNESIUM; MANGANESE; OXYLIPIN; PHYTOHORMONE; VEGETABLE PROTEIN;

ADAPTATION; ARTICLE; CAJANUS; DRUG EFFECT; ENZYMOLOGY; HYDROLYSIS; METABOLISM; MOLECULAR WEIGHT; PH; PLANT DISEASE; PLANT LEAF; TEMPERATURE;

ACETIC ACIDS; ADAPTATION, PHYSIOLOGICAL; CAJANUS; CYCLOPENTANES; ENZYME INHIBITORS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; LEUCYL AMINOPEPTIDASE; MAGNESIUM; MANGANESE; MOLECULAR WEIGHT; OXYLIPINS; PLANT DISEASES; PLANT GROWTH REGULATORS; PLANT LEAVES; PLANT PROTEINS; TEMPERATURE;

CAJAN; CAJANUS CAJAN; FABACEAE;

EID: 79955850350     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2011.02.023     Document Type: Article

References (38)

1. McDonald J.K., Barrett A.J. Mammalian Proteases. A Glossary and Bibliography 1986, vol. 2. Academic Press, London.
2. Walling L.L., Gu Y.-Q. Plant aminopeptidase: occurrence, function and characterization. Aminopeptidase 1996, 174-219. R.G. Landes, Georgetown, Texas. A. Taylor (Ed.).
3. Rendueles P.S., Wolf D.H. Proteinase function in yeast: biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryotic cell. FEMS Microbiol. Rev. 1988, 54:17-46.
4. Matsui M., Fowler J.H., Walling L.L. Leucine aminopeptidases: diversity in structure and function. Biol. Chem. 2006, 387:1536-1544.
5. Rawlings N.D., Barrett A.J. Introduction: metallopeptidases and their clans. Handbook of Proteolytic Enzymes 2004, 231-263. Elsevier/Academic Press, USA. second ed.
6. Bartling D., Weiler E.W. Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants. Eur. J. Biochem. 1992, 205:425-431.
7. Hildmann T., Ebneth M., Pena-Cortes H., Sanchez-Serrano J.J., Willmitzer L., Prat S. General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding. Plant Cell 1992, 4:1157-1170.
8. Pautot V., Holzer F.M., Reisch B., Walling L.L. Leucine aminopeptidase: an inducible component of defense response in Lycopersicon esculentum (tomato). Proc. Natl. Acad. Sci. U.S.A. 1993, 90:9906-9910.
9. Gu Y.-Q., Pautot V., Holzer F.M., Walling L.L. A complex array of proteins related to the multimeric leucine aminopeptidase of tomato. Plant Physiol. 1996, 110:1257-1266.
10. Chao W.S., Pautot V., Holzer F.M., Walling L.L. Leucine aminopeptidase: the ubiquity of LAP-N and specificity of LAP-A. Planta 2000, 210:563-573.
11. Bartling D., Nosek J. Molecular and immunological characterization of leucine aminopeptidase in Arabidopsis thaliana: a new antibody suggests a semi-constitutive regulation of a phytogenetically old enzyme. Plant Sci. 1994, 9:199-209.
12. Mikkonen A. Purification and characterization of leucine aminopeptidase from kidney bean cotyledons. Physiol. Plant 1992, 84:393-398.
13. Sopanen T., Mikola J. Purification and partial characterization of barley leucine aminopeptidase. Plant Physiol. 1975, 55:809-814.
14. Chao W.S., Gu Y.-Q., Pautot V., Bray E.A., Walling L.L. Leucine aminopeptidase RNAs, proteins and activities increase in response to water deficit, salinity and the wound signals-systemin, methyl jasmonate, and abscisic acid. Plant Physiol. 1999, 120:979-992.
15. Milligan S.B., Gasser C.S. Nature and regulation of pistil expressed genes in tomato. Plant Mol. Biol. 1995, 28:691-711.
16. Ruõâz-Rivero O., Prat S. A 2308 deletion of the tomato LAP promoters is able to direct flower-specific and MeJA-induced expression in transgenic plants. Plant Mol. Biol. 1998, 36:639-648.
17. Melbye S.W., Carpenter F.H. Leucine aminopeptidase (bovine lens). Stability and size of subunits. J. Biol. Chem. 1971, 246:2459-2463.
18. Schaller A., Bergey D.R., Ryan C.A. Induction of wound response genes in tomato leaves by bestatin, an inhibitor of aminopeptidases. Plant Cell 1995, 7:1893-1898.
19. Hartle M., Hogler M., Schmidt D.D., Baldwin I.T. Optimized virus-induced gene silencing in Solanum nigrum reveals the defensive function of leucine aminopeptidase against herbivore and the shortcoming of empty vector controls. New Phytol. 2008, 179:356-365.
20. Fowler J.H., Narváez-Vásquez J., Aromdee D.N., Pautot V., Holzer F.M., Walling L.L. Leucine aminopeptidase regulates defense and wound signaling in tomato downstream of jasmonic acid. Plant Cell 2009, 21:1239-1251.
21. Schaller A. A cut above the rest: the regulatory function of plant proteases: a recent and comprehensive survey of the peptidases in plants. Planta 2004, 220:183-197.
22. Beers E.P., Jones A.M., Dickerman A.W. The S8 serine, C1A cysteine and AI aspartic protease families in Arabidopsis. Phytochemistry 2004, 65:43-58.
23. Van der Hoorn R.A.L., Jones J.D. The plant proteolytic machinery and its role in defence. Curr. Opin. Plant Biol. 2004, 7:400-407.
24. Yamauch Y., Ejiri Y., Tanaka K. Purification of an aminopeptidase preferentially releasing N-terminal alanine from cucumber leaves and its identification as a plant aminopeptidase N. Biosci. Biotech. Biochem. 2001, 65(12):2802-2805.
25. Waters S.P., Dalling M.J. Isolation and some properties of an aminopeptidase from primary leaf of wheat (Triticum aestivum L.). Plant Physiol. 1984, 75:118-124.
26. Andersson L., MacNeela J., Wolfenden R. Use of secondary isotope effects and varying pH to investigate the mode of binding of inhibitory amino aldehydes by leucine aminopeptidase. Biochemistry 1985, 24:330-333.
27. Kim H., Lipscomb W.N. Structure and mechanism of bovine lens leucine aminopeptidase. Adv. Enzymol. Relat. Areas Mol. Biol. 1994, 68:153-213.
28. Chen H., Gonzales-Vigil E., Wilkerson C.G., Howe G.A. Stability of plant defense proteins in the gut of insect herbivores. Plant Physiol. 2007, 143:1954-1967.
29. Jiang B., Siregar U., Willeford K.O., Luthe D.S., Williams W.P. Association of a 33-kilodalton cysteine proteinase found in corn callus with the inhibition of fall armyworm larval growth. Plant Physiol. 1995, 108:1631-1640.
30. Lomate P.R., Hivrale V.K. Partial purification and characterization of Helicoverpa armigera (Lepidoptera: Noctuidae) active aminopeptidase secreted in midgut. Comp. Biochem. Physiol. B 2010, 155:164-170.
31. Gu Y.-Q., Holzer F.M., Walling L.L. Overexpression, purification and biochemical characterization of the wound induced leucine aminopeptidase of tomato. Eur. J. Biochem. 1999, 263:726-735.
32. Kim H., Lipscomb W.N. Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by X-ray crystallography. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:5006-5010.
33. Kessler A., Baldwin I.T. Defensive function of herbivore-induced plant volatile emissions in nature. Science 2001, 291:2141-2144.
34. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193:453-464.
35. Hivrale V.K., Chougule N.P., Chhabda P.J., Giri A.P., Kachole M.S. Unrevealing biochemical properties of cockroach (Periplaneta americana) proteinases with gel-X-ray film contact print method. Comp. Biochem. Physiol. B 2005, 141:261-266.
36. Davis B.J. Disc electrophoresis II. Methods and application to human serum. Ann. N. Y. Acad. Sci. 1964, 121:404-427.
37. Bozic N., Vujcic Z. Detection and quantification of leucyl aminopeptidase after native electrophoresis using leucine ρ-nitroanilide. Electrophoresis 2005, 26:2476-2480.
38. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.