Crystal structure of the endopolygalacturonase from the phytopathogenic fungus Colletotrichum lupini and its interaction with polygalacturonase- inhibiting proteins

Proteins: Structure, Function and Genetics

Volumn 70, Issue 1, 2008, Pages 294-299

  Bonivento, Daniele ^a   Pontiggia, Daniela ^a   Di Matteo, Adele ^a   Fernandez Recio, Juan ^b   Salvi, Gianni ^a   Tsernoglou, Demetrius ^a   Cervone, Felice ^a   De Lorenzo, Giulia ^a   Federici, Luca ^c  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b BARCELONA SUPERCOMPUTING CENTER   (Spain)

^c UNIVERSITY OF CHIETI   (Italy)

Author keywords

Glycosyl hydrolase; Leucine rich repeat; Parallel helix; Pectin degradation; Plant innate immunity

Indexed keywords

INHIBITOR PROTEIN; POLYGALACTURONASE;

ARTICLE; COLLETOTRICHUM; COLLETOTRICHUM LUPINI; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALLOGRAPHY; ENZYME ACTIVITY; FUNGUS; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

BASE SEQUENCE; COLLETOTRICHUM; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; FUNGAL PROTEINS; PLANTS; POLYGALACTURONASE; PROTEIN CONFORMATION;

COLLETOTRICHUM LUPINI; FUNGI;

EID: 37349092304     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21610     Document Type: Article

References (28)

1. De Lorenzo G, D'Ovidio R, Cervone F. The role of polygalacturonase- inhibiting proteins (PGIPs) in defense against pathogenic fungi. Ann Rev Phytopathol 2001;39:313-335.
2. Kars I, Krooshof GH, Wagemakers L, Joosten R, Benen JA, van Kan JA. Necrotizing activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris. Plant J 2005;43:213-225.
3. Cervone F, Hahn MG, De Lorenzo G, Darvill A, Albersheim P. Host-pathogen interactions. XXXIII. A plant protein converts a fungal pathogenesis factor into an elicitor of plant defense responses. Plant Physiol 1989;90:542-548.
4. Ridley BL, O'Neill MA, Mohnen D. Pectins: structure, biosynthesis, and oligogalacturonide-related signaling. Phytochemistry 2001;57: 929-967.
5. Kobe B, Kajava AV. The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 2001;11:725-732.
6. D'Ovidio R, Raiola A, Capodicasa C, Devoto A, Pontiggia D, Roberti S, Galletti R, Conti E, O'Sullivan D, De Lorenzo G. Characterization of the complex locus of bean encoding polygalacturonase-inhibiting proteins reveals subfunctionalization for defense against fungi and insects. Plant Physiol 2004;135:2424-2435.
7. D'Ovidio R, Roberti S, Di Giovanni M, Capodicasa C, Melaragni M, Sella L, Tosi P, Favaron F. The characterization of the soybean polygalacturonase- inhibiting proteins (Pgip) gene family reveals that a single member is responsible for the activity detected in soybean tissues. Planta 2006;224:633-645.
8. Federici L, Di Matteo A, Fernandez-Recio J, Tsernoglou D, Cervone F. Polygalacturonase inhibiting proteins: players in plant innate immunity? Trends Plant Sci 2006;11:65-70.
9. Ferrari S, Galletti R, Vairo D, Cervone F, De Lorenzo G. Antisense expression of the Arabidopsis thaliana AtPGIP1 gene reduces polygalacturonase- inhibiting protein accumulation and enhances susceptibility to Botrytis cinerea. Mol Plant Microbe Interact 2006;19:931-936.
10. Federici L, Caprari C, Mattei B, Savino C, Di Matteo A, De Lorenzo G, Cervone F, Tsernoglou D. Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein). Proc Natl Acad Sci USA 2001;98:13425-13430.
11. King D, Bergmann C, Orlando R, Benen JA, Kester HC, Visser J. Use of amide exchange mass spectrometry to study conformational changes within the endopolygalacturonase II-homogalacturonan-polygalacturonase inhibiting protein system. Biochemistry 2002;41: 10225-10233.
12. Sicilia F, Fernandez-Recio J, Caprari C, De Lorenzo G, Tsernoglou D, Cervone F, Federici L. The polygalacturonase-inhibiting protein PGIP2 of Phaseolus vulgaris has evolved a mixed mode of inhibition of endopolygalacturonase PG1 of Botrytis cinerea. Plant Physiol 2005;139:1380-1388.
13. Oelofse D, Dubery IA, Meyer R, Arendse MS, Gazendam I, Berger DK. Apple polygalacturonase inhibiting protein1 expressed in transgenic tobacco inhibits polygalacturonases from fungal pathogens of apple and the anthracnose pathogen of lupins. Phytochemistry 2006;67:255-263.
14. Ochman H, Gerber AS, Hartl DL. Genetic applications of an inverse polymerase chain reaction. Genetics 1998;120:621-623.
15. Milner Y, Avigad G. A copper reagent for the determination of hexuronic acids and certain ketohexoses. Carbohydr Res 1967;4:359-361.
16. Di Matteo A, Federici L, Mattei B, Salvi G, Johnson KA, 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 USA 2003; 100:10124-10128.
17. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
18. Read RJ. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr D Biol Crystallogr 2001;57: 1373-1382.
19. Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997;53:240-255.
20. Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004;60:2126-2132.
21. Winn MD, Isupov MN, Murshudov GN. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr D Biol Crystallogr 2001;57:122-133.
22. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK - a program to check the sterochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
23. Shindyalov IN, Bourne PE. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng 1998;11:739-747.
24. Fernandez-Recio J, Totrov M, Skorodumov C, Abagyan R. Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins 2005;58:134-143.
25. Pickersgill R, Smith D, Worboys K, Jenkins J. Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora. J Biol Chem 1998;273:24660-24664.
26. van Santen Y, Benen JA, Schroter KH, Kalk KH, Armand S, Visser J, Dijkstra BW. 1.68-Å crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis. J Biol Chem 1999;274:30474-30480.
27. Armand S, Wagemaker MJ, Sanchez-Torres P, Kester HC, van Santen Y, Dijkstra BW, Visser J, Benen JA. The active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis. J Biol Chem 2000;275:691-696.
28. Stotz HU, Bishop JG, Bergmann CW, Koch M, Albersheim P, Darvill AG, Labavitch JM. Identification of target amino acids that effect interactions of fungal polygalacturonases and their plant inhibitors. Physiol Mol Plant Pathol 2000;56:117-130.