title: Elicitors and suppressors of hydroxyproline-rich glycoprotein accumulation are solubilized from plant cell walls by endopolygalacturonase.
abstract: Treatment of bean cell walls with a pure endopolygalacturonase of the bean pathogen Colletotrichum lindemuthianum race beta released oligogalacturonides and pectic fragments which were separated according to their charge and size. Among galacturonic-acid-containing components, elicitors and suppressors of the plant cell wall hydroxyproline-rich glycoprotein (HRGP) were recovered. Two active small oligogalacturonides with degrees of polymerization of 2 and 3 were characterized by high-performance anion-exchange-chromatography pulsed amperometric detection and fast-atom-bombardment mass spectrometry; they elicited 40-70% hydroxyproline increase within 48 hours at 450 nmol/bean cutting. In contrast, pectic fragments of higher molecular mass, predominantly composed of galacturonic acid and containing sugars typical of the rhamnogalacturonan II domain of pectic polysaccharides, had the ability to substantially suppress hydroxyproline deposition. Maximum suppressor activity, 30-40% below the activity of the control, occurred in 48 hours. In view of the low one-cycle turnover of these proteins in the cell wall and of their structural role, these changes might significantly affect cell wall properties. Elicitation and/or suppression of hydroxyproline were correlated to modifications of HRGP-extensin gene expression. Northern-blot analysis of RNA showed that changes in the transcript intensity became clearly visible within the first 12 hours after the start of either treatment. The results show that pectic components of the plant extracellular matrix have the potential to regulate wall matrix biogenesis. Implications of this finding in plant defense and development are discussed.
authors.affiliation: Centre de Biologie et Physiologie Végétale, UA CNRS n. 1941, Université Paul Sabatier, Toulouse, France.
authors.forename: G
authors.initials: G
authors.lastname: Boudart
authors.forename: G
authors.initials: G
authors.lastname: Dechamp-Guillaume
authors.forename: C
authors.initials: C
authors.lastname: Lafitte
authors.forename: G
authors.initials: G
authors.lastname: Ricart
authors.forename: J P
authors.initials: JP
authors.lastname: Barthe
authors.forename: D
authors.initials: D
authors.lastname: Mazau
authors.forename: M T
authors.initials: MT
authors.lastname: Esquerré-Tugayé
mesh_terms: D002473:Cell Wall / Q000187:drug effects / Q000378:metabolism; D007887:Fabaceae / Q000235:genetics / Q000378:metabolism / Q000382:microbiology; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D003904:Mitosporic Fungi / Q000201:enzymology / Q000472:pathogenicity; D009844:Oligosaccharides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D010368:Pectins / Q000302:isolation & purification / Q000494:pharmacology; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D010946:Plants, Medicinal; D011096:Polygalacturonase / Q000494:pharmacology*; D015398:Signal Transduction; D012995:Solubility
chemical_list: D006023:Glycoproteins; D009844:Oligosaccharides; D010940:Plant Proteins; C005488:extensin protein, plant; D010368:Pectins; D011096:Polygalacturonase