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Characterization of the complex locus of bean encoding polygalacturonase- inhibiting proteins reveals subfunctionalization for defense against fungi and insects

TitleCharacterization of the complex locus of bean encoding polygalacturonase- inhibiting proteins reveals subfunctionalization for defense against fungi and insects
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2004
AuthorsD’Ovidio, R., Raiola A., Capodicasa Cristina, Devoto A., Pontiggia D., Roberti S., Galletti R., Conti E., O’Sullivan D., and De Lorenzo G.
JournalPlant Physiology
Pagination2424 - 2435
Date Published2004
ISBN Number00320889 (ISSN)
KeywordsAdelphocoris, Adelphocoris lineolatus, Amino Acid, Amino Acid Sequence, Amino acids, animal, Animals, article, bean, chemistry, Disease control, Diseases, Elicitors, Eukaryota, Fungi, fungus, Fusarium, Genes, genetics, Genome, genotype, Gibberella fujikuroi, Hexapoda, Immunity, innate immunity, insect, insecta, Insects, Lygus, Lygus rugulipennis, metabolism, microbiology, molecular genetics, Molecular Sequence Data, Natural, nucleotide sequence, parasitology, Pathogenic fungi, Pathology, PGIP protein, Phaseolus, Phaseolus (angiosperm), Phaseolus vulgaris, Plant, plant disease, Plant Diseases, Plant Proteins, Plants, Plants (botany), Proteins, Sequence Alignment, sequence homology, vegetable protein

Polygalacturonase-inhibiting proteins (PGIPs) are extracellular plant inhibitors of fungal endopolygalacturonases (PGs) that belong to the superfamily of Leu-rich repeat proteins. We have characterized the full complement of pgip genes in the bean (Phaseolus vulgaris) genotype BAT93. This comprises four clustered members that span a 50-kb region and, based on their similarity, form two pairs (Pvpgip1/Pvpgip2 and Pvpgip3/Pvpgip4). Characterization of the encoded products revealed both partial redundancy and subfunctionalization against fungal-derived PGs. Notably, the pair PvPGIP3/PvPGIP4 also inhibited PGs of two mirid bugs (Lygus rugulipennis and Adelphocoris lineolatus). Characterization of Pvpgip genes of Pinto bean showed variations limited to single synonymous substitutions or small deletions. A three-amino acid deletion encompassing a residue previously identified as crucial for recognition of PG of Fusarium moniliforme was responsible for the inability of BAT93 PvPGIP2 to inhibit this enzyme. Consistent with the large variations observed in the promoter sequences, reverse transcription-PCR expression analysis revealed that the different family members differentially respond to elicitors, wounding, and salicylic acid. We conclude that both biochemical and regulatory redundancy and subfunctionalization of pgip genes are important for the adaptation of plants to pathogenic fungi and phytophagous insects.


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