Specificity of the wound-induced leucine aminopeptidase (LAP-A) of tomato: Activity on dipeptide and tripeptide substrates

European Journal of Biochemistry

Volumn 267, Issue 4, 2000, Pages 1178-1187

  Gu, Yong Qiang ^a,b   Walling, Linda L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b United States Department of Agriculture Agricultural Research Service and Boyce Thompson Institute for Plant Research   (United States)

Author keywords

Aminopeptidases; Defense; Exopeptidases; Protein degradation; Wounding

Indexed keywords

AMINOPEPTIDASE; CYTOSOL AMINOPEPTIDASE; PEPTIDASE;

ARTICLE; ENZYME PURIFICATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE OVEREXPRESSION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; TOMATO;

ANIMALS; DIPEPTIDES; ESCHERICHIA COLI; HYDROLYSIS; KINETICS; LEUCYL AMINOPEPTIDASE; LYCOPERSICON ESCULENTUM; OLIGOPEPTIDES; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; SWINE; THERMODYNAMICS;

ANIMALIA; ESCHERICHIA COLI; LYCOPERSICON ESCULENTUM; PROKARYOTA; SUIDAE;

EID: 0033984169     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01116.x     Document Type: Article

References (55)

1. 2+ of the zinc metalloenzyme, amino acid composition, and sulfhydryl content. J. Biol. Chem. 248, 294-304.
2. 2. Kim, H. & Lipscomb, W.N. (1994) Structure and mechanism of bovine lens leucine aminopeptidase. Adv. Enzymol. Rel. Areas Molec. Biol. 68, 153-213.
3. 3. Taylor, A., Sanford, D. & Nowell, T. (1996) Structure and function of bovine lens aminopeptidase and comparison with homologous aminopeptidases. In Aminopeptidases (Taylor, A., ed.), pp. 21-67. R. G. Landes Co., Austin, TX, USA.
4. 4. Sträter, N. & Lipscomb, W.N. (1995) Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form. Biochemistry 34, 9200-9210.
5. 5. Bartling, D. & Weiler, E.W. (1992) Leucine aminopeptidase from Arabidopsis thaliana - molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants. Eur. J. Biochem. 205, 425-431.
6. 6. Hildmann, T., Ebneth, M., Peña-Cortes, H., Sanchez-Serrano, J.J., Willmitzer, L. & Prat, S. (1992) General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding. Plant Cell 4, 1157-1170.
7. 7. Pautot, V., Holzer, F.M., Reisen, B. & Walling, L.L. (1993) Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato). Proc. Natl Acad. Sci. USA 90, 9906-9910.
8. 8. Gu, Y.Q., Chao, W.S. & Walling, L.L. (1996) Localization and post-translational processing of the wound-induced leucine amino-peptidase proteins of tomato. J. Biol. Chem. 271, 25880-25887.
9. 9. Vogt, V.M. (1970) Purification and properties of an aminopeptidase from Escherichia coli. J. Biol. Chem. 245, 4760-4769.
10. 10. Stirling, C.J., Colloms, S.D., Collins, J.F., Szatmari, G. & Sherratt, D.J. (1989) xerB, an Escherichia coli gene required for plasmid ColEl site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase. EMBO J. 8, 1623-1627.
11. 11. Taylor, A., Daims, M., Lee, J. & Surgenor, T. (1982) Identification and quantification of leucine aminopeptidase in aged normal and cataractous human lenses and ability of bovine lens LAP to cleave bovine crystallins. Curr. Eye Res. 2, 47-56.
12. 12. Stuart, D.D. & Doughty, M.J. (1996) In vitro UVB irradiation of bovine crystalline lens causes cell damage and reduction in leucine aminopeptidase activity in lens epithelium. J. Photochem. Photobiol. B. Biol. 32, 81-87.
13. 13. Sharma, K.K. & Kester, K. (1996) Peptide hydrolysis in lens - role of leucine aminopeptidase, aminopeptidase III, prolyloligopeptidase and acylpeptidehydrolase. Curr. Eye Res. 15, 363-369.
14. 14. Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl Acad. Sci. USA 93, 12142-12149.
15. 15. Bradshaw, R.A., Brickey, W.W. & Walker, K.W. (1998) N-terminal processing: the methionine aminopeptidase and N-α-acetyl transferase families. Trends Biochem. Sci. 23, 263-267.
16. 16. Beninga, J., Rock, K.L. & Goldberg, A.L. (1998) Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273, 18734-18742.
17. 17. Harris, C.A., Hunte, B., Krauss, M.R., Taylor, A. & Epstein, L.B. (1992) Induction of leucine aminopeptidase by interferon-γ - identification by protein microsequencing after purification by preparative 2-dimensional gel electrophoresis. J. Biol. Chem. 267, 6865-6869.
18. 18. Mikkonen, A. (1992) Purification and characterization of leucine aminopeptidase from kidney bean cotyledons. Physiol. Plant. 84, 393-398.
19. 19. Sopanen, T. & Mikola, J. (1975) Purification and partial characterization of barley leucine aminopeptidase. Plant Physiol. 55, 809-814.
20. 20. Gu, Y.Q., Pautot, V., Holzer, F.M. & Walling, L.L. (1996) A complex array of proteins related to the multimeric leucine aminopeptidase of tomato. Plant Physiol. 110, 1257-1266.
21. 21. Chao, W.S., Gu, Y.-Q., Pautot, V., Bray, E.A. & Walling, L.L. (1999) 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. 120, 979-992.
22. 22. Gu, Y.-Q., Holzer, F.M. & Walling, L.L. (1999) Over-expression, purification and biochemical characterization of the wound-induced leucine aminopeptidase of tomato. Eur. J. Biochem. 263, 726-735.
23. 23. Bartling, D. & Nosek, J. (1994) Molecular and immunological characterization of leucine aminopeptidase in Arabidopsis thaliana: a new antibody suggests a semi-constitutive regulation of a phylogenetically old enzyme. Plant Sci. 99, 199-209.
24. 24. Chao, W.S., Pautot, V., Holzer, F.M. & Walling, L.L. (2000) Leucine aminopeptidases: The ubiquity of LAP-N and the specificity of LAP-A. Planta in press.
25. 25. Milligan, S.B. & Gasser, C.S. (1995) Nature and regulation of pistil-expressed genes in tomato. Plant Mol. Biol. 28, 691-711.
26. 26. Walling, L.L. & Gu, Y.-Q. (1996) Plant aminopeptidases: occurrence, function and characterization. In Aminopeptidases (Taylor, A., ed.), pp. 174-219. R. G. Landes Co., Georgetown, TX, USA.
27. 27. Inze, D. & Van Montagu, M. (1995) Oxidative stress in plants. Curr. Opin. Biotech. 6, 153-158.
28. 28. Davies, W.J. & Mansfield, T.A. (1983) The role of abscisic acid in drought avoidance. In Abscisic Acid (Addicott, F.T., ed.), pp. 237-268. Praeger, New York, USA.
29. 29. Davies, M.J., Fu, S. & Dean, R.T. (1995) Protein hydroperoxides can give rise to reactive free radicals. Biochem. J. 305, 643-649.
30. 30. McCulloch, R., Burke, M.E. & Sherratt, D.J. (1994) Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination. Mol. Microbiol. 12, 241-251.
31. 31. Ramagli, L.S. & Rodriguez, L.V. (1985) Quantitation of microgram amounts of protein in two-dimensional polyacrylamide gel electrophoresis sample buffer. Electrophoresis 6, 559-563.
32. 32. Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
33. 33. Oettgen, H.C. & Taylor, A. (1985) Purification, preliminary characterization, and immunological comparison of hog lens leucine aminopeptidase (EC 3.4.11.1) with hog kidney and beef lens aminopeptidases. Anal. Biochem. 146, 238-245.
34. 34. Binkley, F., Leibach, F. & King, N. (1968) A new method of peptidase assay and the separation of three leucylglycinases of renal tissues. Arch. Biochem. Biophys. 128, 397-405.
35. 35. Schechter, I. & Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Comm. 27, 157-162.
36. 36. Barrett, A.J. (1994) Classification of peptidases. Methods Enzymol. 244, 1-15.
37. 37. Van Wart, H.E. & Lin, S.H. (1981) Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney leucine aminopeptidase. Biochemistry 20, 5682-5689.
38. 38. Smith, E.L. & Solnim, N.B. (1948) The specificity of leucine aminopeptidase. J. Biol. Chem. 176, 835-841.
39. 39. Hanson, H. & Frohne, M. (1976) Crystalline leucine aminopeptidase from lens (alpha-aminoacyl-peptide hydrolase; EC 3.4.11.1). Methods Enzymol. 45, 504-520.
40. 40. Smith, E.L. & Bergmann, M. (1944) The peptidases of intestinal mucosa. J. Biol. Chem. 153, 627-651.
41. 41. Smith, E.L. & Polgase, W.J. (1949) The specificity of leucine aminopeptidase II. Optical and sidechain specificity. J. Biol. Chem. 180, 1209-1223.
42. 42. Smith, E.L., Spackman, D.H. & Polgase, W.J. (1952) The specificity of leucine aminopeptidase III. Action of diastereoisomers. J. Biol. Chem. 199, 801-817.
43. 43. Smith, E.L. & Spackman, D.H. (1955) Leucine aminopeptidase V. J. Biol. Chem. 212, 271-299.
44. 44. Turzynski, A. & Mentlein, R. (1990) Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase. Eur. J. Biochem. 190, 509-515.
45. 45. Wiederanders, B., Lasch, J., Kirschke, H., Bohley, P., Ansorge, S. & Hanson, H. (1973) The suitability of bovine-lens leucine aminopeptidase for sequence analysis and limited hydrolysis of polypeptides. Eur. J. Biochem. 36, 504-508.
46. 46. Botbol, V. & Scornik, O.A. (1983) Peptide intermediates in the degradation of cellular proteins. Bestatin permits their accumulation in mouse liver in vivo. J. Biol. Chem. 258, 1942-1949.
47. 47. Botbol, V. & Scornik, O.A. (1979) Degradation of abnormal proteins in intact mouse reticulocytes: accumulation of intermediates in the presence of bestatin. Proc. Natl Acad. Sci. USA 76, 710-713.
48. 48. Deftos, L.J. & Potts, J.T. Jr (1969) Contamination of DFP-treated leucine aminopeptidase with multiple endopeptidases. Biochim. Biophys. Acta 171, 121-127.
49. 49. Schaller, A. & Ryan, C.A. (1996) Systemin: a polypeptide defense signal in plants. Bioessays 18, 27-33.
50. 50. Constabel, C.P., Yip, L. & Ryan, C.A. (1998) Prosystemin from potato, black nightshade, and bell pepper: Primary structure and biological activity of predicted system in polypeptides. Plant Mol. Biol. 36, 55-62.
51. 51. McGurl, B., Pearce, G., Orozco-Cardenas, M. & Ryan, C.A. (1992) Structure, expression, and antisense inhibition of the systemin precursor gene. Science 255, 1570-1573.
52. 52. Bachmair, A., Becker, F. & Schell, J. (1993) Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin-dependent protein degradation. Proc. Natl Acad. Sci. USA 90, 418-421.
53. 53. Callis, J. (1995) Regulation of protein degradation. Plant Cell 7, 845-857.
54. 54. Vierstra, R.D. (1996) Proteolysis in plants: mechanisms and functions. Plant Mol. Biol. 32, 275-302.
55. 55. Worley, C.K., Ling, R. & Callis, J. (1998) Engineering in vivo instability of firefly luciferase and Escherichia coli beta-glucuronidase in higher plants using recognition elements from the ubiquitin pathway. Plant Mol. Biol. 37, 337-347.