Crystal structure of the endopolygalacturonase from the phytopathogenic fungus <i>Colletotrichum lupini</i> and its interaction with polygalacturonase‐inhibiting proteins

Bonivento, Daniele; Pontiggia, Daniela; Matteo, Adele Di; Fernández‐Recio, Juan; Salvi, G.; Tsernoglou, Demetrius; Cervone, Felice; Lorenzo, Giulia De; Federici, L.

doi:10.1002/prot.21610

Cited by 50 publications

(47 citation statements)

References 28 publications

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“…Comparing to AtPGIP1 containing ten LRR repeats, CbPGIP1 contained one N-terminal LRR repeat and a set of eight LRR repeats, which would be involved in the function of CbPGIP1 to biotic and some abiotic stresses. In plants, LRR acts as a prominent defense reactive molecule Bonivento et al 2008;Cheng et al 2008) and plays a relevant role in both, resistance and development (Jang et al 2003;Li et al 2003). Furthermore, signal transduction in plants toward activating defense The assays were performed on cDNA synthesized from RNA isolated from calli induced by S. solani and SA at diVerent times.…”

Section: Discussionmentioning

confidence: 97%

Molecular cloning, functional analysis and localization of a novel gene encoding polygalacturonase-inhibiting protein in Chorispora bungeana

Chen

Feng

et al. 2009

Planta

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Polygalacturonase-inhibiting proteins (PGIPs) are plant defense proteins. To date, no spatial distribution of PGIPs and interaction between PGIPs and nitric oxide (NO) in plant were described. Here, we first reported the full-length cDNA sequence of PGIP of Chorispora bungeana (CbPGIP1). Notably, immunofluorescence localization showed that the CbPGIP was evenly distributed in leaves but it was mainly localized in epidermis and vascular bundle in stems and roots. Further studies indicated that CbPGIP had higher abundance in roots than in stems and leaves. Conversely, the bulk PGIP of C. bungeana showed a higher activity in leaves than in stems and roots. In addition, quantitative real-time polymerase chain reaction demonstrated that CbPGIP1 expression was induced by Stemphylium solani, salicylic acid (SA), 4, -4 degrees C and NO. This is a first report attempting to predict if NO can induce the PGIP expression. Taken together, these findings showed that the gene was spatially regulated and NO and SA might take part in CbPGIP1 expression induced by biotic and abiotic stresses. This study highlighted the potential importance of CbPGIP1 and NO in plant resistance.

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Section: Discussionmentioning

confidence: 97%

Molecular cloning, functional analysis and localization of a novel gene encoding polygalacturonase-inhibiting protein in Chorispora bungeana

Chen

Feng

et al. 2009

Planta

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“…PGs are extremely variable in terms of shape and electrostatic surfaces as well as desolvation energy surfaces, although maintaining the same overall fold (31,33) and single PGIPs (i.e., PvPGIP2) can inhibit different PGs with different mechanisms, either competitive or noncompetitive. These features lead us to propose that in the diverse PvPGIP2-PG pairs different sets of contacts take place, possibly involving different surface areas and residues of the PG ligands (21).…”

Section: Discussionmentioning

confidence: 99%

“…Single PGIP residues located in the concave surface of the LRR solenoid (i.e., the ␤-sheet B1) differentially affect the inhibition of fungal PGs (23,31). PGIPs of several plant species, as well as single PGIPs, show different inhibition kinetics toward various fungal PGs (31)(32)(33)(34). Consistently, molecular-docking simulations of PG-PGIP complexes suggested that PGIP isoform 2 from Phaseolus vulgaris (PvPGIP2) binds the various PG partners in different areas of their surface (21).…”

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confidence: 99%

Integration of evolutionary and desolvation energy analysis identifies functional sites in a plant immunity protein

Casasoli

Federici

Spinelli

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Plant immune responses often depend on leucine-rich repeat receptors that recognize microbe-associated molecular patterns or pathogen-specific virulence proteins, either directly or indirectly. When the recognition is direct, a molecular arms race takes place where plant receptors continually and rapidly evolve in response to virulence factor evolution. A useful model system to study ligand-receptor coevolution dynamics at the protein level is represented by the interaction between pathogen-derived polygalacturonases (PGs) and plant polygalacturonase-inhibiting proteins (PGIPs). We have applied codon substitution models to PGIP sequences of different eudicotyledonous families to identify putative positively selected sites and then compared these sites with the propensity of protein surface residues to interact with protein partners, based on desolvation energy calculations. The 2 approaches remarkably correlated in pinpointing several residues in the concave face of the leucine-rich repeat domain. These residues were mutated into alanine and their effect on the recognition of several PGs was tested, leading to the identification of unique hotspots for the PGIP-PG interaction. The combined approach used in this work can be of general utility in cases where structural information about a pattern-recognition receptor or resistancegene product is available.adaptive evolution ͉ molecular recognition ͉ plant-pathogen interactions ͉ protein-protein interactions ͉ polygalacturonase-inhibiting protein (PGIP)

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“…(Cary, Brown, Cleveland, Whitehead, & Dean, 1995), Penicillium janthinellum (Iguch, Hirano, Kishida, Kawasaki, & Sakai, 1997) and A. fumigatus (Fedorova et al, 2008), respectively. With the crystal structures of endo-polygalacturonases 2IQ7 (66% identity; Bonivento et al, 2008) and 1NHC (82% identity; (van Pouderoyen, Snijder, Benen, & Dijkstra, 2003) as templates, NfPG I and NfPG II were predicted to fold into a right-handed parallel b-helix with ten complete turns. Four conserved catalytic residues of GH 28 endo-polygalacturonases, Asp 182 , Asp 203 , Asp 204 and His 225 for NfPG I and Asp 186 , Asp 207 , Asp 208 and His 229 for NfPG II, were identified (van Santen et al, 1999), respectively.…”

Section: Gene Cloning and Sequence Analysismentioning

confidence: 99%

Biochemical characterization of three distinct polygalacturonases from Neosartorya fischeri P1

Pan

et al. 2015

Food Chemistry

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

Cited by 50 publications

References 28 publications

Molecular cloning, functional analysis and localization of a novel gene encoding polygalacturonase-inhibiting protein in Chorispora bungeana

Molecular cloning, functional analysis and localization of a novel gene encoding polygalacturonase-inhibiting protein in Chorispora bungeana

Integration of evolutionary and desolvation energy analysis identifies functional sites in a plant immunity protein

Biochemical characterization of three distinct polygalacturonases from Neosartorya fischeri P1

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