Modes of action of five different endopectate lyases from Erwinia chrysanthemi 3937

Journal of Bacteriology

Volumn 181, Issue 12, 1999, Pages 3705-3709

  Roy, Caroline ^a,b   Kester, Harry ^a   Visser, Jaap ^a   Shevchik, Vladimir ^b   Hugouvieux Cotte Pattat, Nicole ^b   Robert Baudouy, Jeanine ^b   Benen, Jacques ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PECTATE LYASE; POLYGALACTURONIC ACID;

ARTICLE; DEPOLYMERIZATION; ENZYME ACTIVITY; ERWINIA; NONHUMAN; PH; PRIORITY JOURNAL; REACTION ANALYSIS;

EID: 0033016760     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.12.3705-3709.1999     Document Type: Article

References (25)

1. Barras, F., F. Van Gijsegem, and A. K. Chatterjee. 1994. Extracellular enzymes and pathogenesis of soft-rot Erwinia. Annu. Rev. Phytopathol. 32:201-234.
2. Boccara, M., A. Diolez, M. Rouve, and A. Kotoujansky. 1988. The role of individual pectate lyases of Erwinia chrysanthemi strain 3937 in pathogenicity on Saintpaulia plants. Physiol. Mol. Plant Pathol. 33:95-104.
3. Brooks, A. D., S. Y. He, S. Gold, N. T. Keen, A. Collmer, and S. W. Hutcheson. 1990. Molecular cloning of the structural gene for exopolygalacturonate lyase from Erwinia chrysanthemi EC16 and characterization of the enzyme product. J. Bacteriol. 172:6950-6958.
4. De Vries, J. A., M. Hansen, J. Sederberg, P. E. Glahn, and J. K. Pedersen. 1986. Distribution of methoxyl groups in pectins. Carbohydr. Polym. 6:165-176.
5. Henrissat, B., S. E. Heffron, M. D. Yoder, S. E. Lietzke, and F. Jurnak. 1995. Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol. 107:963-976.
6. Hugouvieux-Cotte-Pattat, N., G. Condemine, W. Nasser, and S. Reverchon. 1996. Regulation of pectinolysis in Erwinia chrysanthemi. Annu. Rev. Microbiol. 50:213-257.
7. Kester, H. C. M., and J. Visser. 1990. Purification and characterization of polygalacturonases produced by the hyphal fungus Aspergillus niger. Biotechnol. Appl. Biochem. 12:150-160.
8. Kester, H. C. M., M. A. Kusters-van Someren, Y. Müller, and J. Visser. 1996. Primary structure and characterization of an exopolygalacturonase from Aspergillus tubingensis. Eur. J. Biochem. 240:738-746.
9. Lietzke, S. E., R. D. Scavetta, M. D. Yoder, and F. Jurnak. 1996. The refined three-dimensional structure of pectate lyase E from Erwinia chrysanthemi at 2.2 Å resolution. Plant Physiol. 111:73-92.
10. Lojkowska, E., C. Masclaux, M. Boccara, J. Robert-Baudouy, and N. Hugouvieux-Cotte-Pattat. 1995. Characterization of the pelL gene encoding a novel pectate lyase of Erwinia chrysanthami 3937. Mol. Microbiol. 16:1183-1195.
11. MacMillan, G. P., and R. H. Vaughn. 1964. Purification and properties of a polygalacturonate-trans-eliminase produced by Clostridium multifermentans. Biochemistry 3:564-572.
12. Pařenicová, L., J. A. E. Benen, H. C. M. Kester, and J. Visser. 1998. pgaE encodes a fourth member of the endopolygalacturonase gene family from Aspergillus niger. Eur. J. Biochem. 251:72-80.
13. Pickersgill, R., J. Jenkins, G. Harris, W. Nasser, and J. Robert-Baudouy. 1994. The structure of Bacillus subtilis pectate lyase in complex with calcium. Nat. Struct. Biol. 1:717-723.
14. Pissavin, C., J. Robert-Baudouy, and N. Hugouvieux-Cotte-Pattat. 1996. Regulation of pelZ, a gene of the pelB-pelC cluster encoding a new pectate lyase of Erwinia chrysanthemi 3937. J. Bacteriol. 178:7187-7196.
15. Preston, J. F., J. D. Rice, L. O. Ingram, and N. T. Keen. 1992. Differential depolymerization mechanisms of pectate lyases secreted by Erwinia chrysanthemi EC16. J. Bacteriol. 174:2039-2042.
16. Scavetta, R. D., S. R. Herron, A. T. Hotchkiss, N. Kita, N. T. Keen, J. A. E. Benen, H. C. M. Kester, J. Visser, and F. Jurnak. Structure of plant cell wall fragment complexed to PelC. Plant Cell, in press.
17. Schols, H. A., M. A. Posthumus, and A. G. J. Voragen. 1990. Structural features of hairy regions of pectins isolated from apple juice produced by the liquefaction process. Carbohydr. Res. 206:117-130.
18. Shevchik V. E., M. Scott, O. Mayans, and J. Jenkins. 1998. Crystallization and preliminary X-ray analysis of a member of a new family of pectate lyases, PelL from Erwinia chrysanthemi. Acta Crystallogr. Sect. D. 54:419-422.
19. Shevchik, V. E., and N. Hugouvieux-Cotte-Pattat. 1997. Identification of a bacterial pectin acetyl esterase in Erwinia chrysanthemi. Mol. Microbiol. 24:1285-1301.
20. Shevchik, V. E., J. Robert-Baudouy, and N. Hugouvieux-Cotte-Pattat. 1997. Pectate lyase PelI of Erwinia chrysanthemi 3937 belongs to a new family. J. Bacteriol. 179:7321-7330.
21. Shevchik, V. E., H. C. M. Kester, J. A. E. Benen, J. Visser, J. Robert-Baudouy, and N. Hugouvieux-Cotte-Pattat. 1999. Characterization of the exopolygalacturonate lyase, PelX, of Erwinia chrysanthemi 3937. J. Bacteriol. 181:1652-1663.
22. Shevchik, V. E., G. Condemine, J. Robert-Baudouy, and N. Hugouviouv-Cotte-Pattat. The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of the pectin catabolism in Erwinia chrysanthemi 3937. J. Bacteriol, in press.
23. Tardy, F., W. Nasser, J. Robert-Baudouy, and N. Hugouvieux-Cotte-Pattat. 1997. Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: enzyme characteristics and potential inhibitors. J. Bacteriol. 179: 2503-2511.
24. Yoder, M. D. N. T. Keen, and F. Jurnak. 1993. New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260: 1503-1507.
25. Yoder, M. D., and F. Jurnak. 1995. The refined three-dimensional structure of pectate lyase C from Erwinia chrysanthemi at 2.2 Angstrom resolution. Plant Physiol. 107:349-364.