Expression of exo-polygalacturonases in<i>Botrytis cinerea</i>

Rha, Eugene; Park, Hong Jai; Kim, Myeong Ok; Chung, Young Ryun; Lee, Chang-Won; Kim, Jae Won

doi:10.1111/j.1574-6968.2001.tb10740.x

Cited by 30 publications

(4 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The rate of the enzyme-catalyzed reduction of viscosity (7%) of solutions of pectin as a substrate was considerably lesser than the rate of release of reducing sugars (50%), confirming that this enzyme functioned in an exo-like manner. This result was similar to that reported for PGs from B. cinerea [44] and Bacillus [32] using PGA as a substrate. Furthermore, PGIII 0 and PG 5 enzymes purified from F. oxysporum f. sp.…”

Section: Discussionsupporting

confidence: 92%

Characterization of an Exopolygalacturonase from Aspergillus niger

Fahmy

El-Beih

Mohamed

et al. 2008

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Polygalacturonase (PGI) from Aspergillus niger NRRL3 was purified about 12.0-fold from the cell-free broth using diethylaminoethyl-Sepharose and Sephacryl S-200 columns. The molecular weight of the PGI was 32,000 Da as estimated by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. PGI had an isoelectric point of 7.6 and an optimum pH of 5.0. PGI was active on polygalacturonic acid and esterified pectins, but the activity on pectin decreased with an increase in degree of esterification. PGI had higher affinity (low Km) and turnover number (Vmax/Km and Kcat/Km) toward polygalacturonic acid. PGI was found to have a temperature optimum at 40 degrees C and was approximately stable up to 30 degrees C. All the examined metal cations had partial inhibitory effects on PGI, while Mn+2 at 5 mM caused a complete inhibition for the enzyme. Comparison of viscosity reduction rates with release of reducing sugars indicated that the enzyme from A. niger is exoacting. The storage stability study of PGI showed that the enzyme in powder form retained 56% of its activity after 9 months of storage at 4 degrees C. The above properties of PGI may be suitable for food processing.

show abstract

Section: Discussionsupporting

confidence: 92%

Characterization of an Exopolygalacturonase from Aspergillus niger

Fahmy

El-Beih

Mohamed

et al. 2008

Appl Biochem Biotechnol

View full text Add to dashboard Cite

show abstract

“…The expression of exo-PGs has been previously identified in cucumber leaves inoculated with spores of B. cinerea . 46 This expression either increased with time of culture (exo-PG I) or was transiently expressed soon after the start of culture (exo-PGII), suggesting that the exo-PGs play an important role in pathogenesis at an early stage of infection as well as in tissue maceration of host plants. 46 …”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Ripening Tomato Fruit Infected by Botrytis cinerea

et al. 2012

View full text Add to dashboard Cite

Botrytis cinerea, a model necrotrophic fungal pathogen that causes gray mold as it infects different organs on more than 200 plant species, is a significant contributor to postharvest rot in fresh fruit and vegetables, including tomatoes. By describing host and pathogen proteomes simultaneously in infected tissues, the plant proteins that provide resistance and allow susceptibility and the pathogen proteins that promote colonization and facilitate quiescence can be identified. This study characterizes fruit and fungal proteins solubilized in the B. cinerea−tomato interaction using shotgun proteomics. Mature green, red ripe wild type and ripening inhibited (rin) mutant tomato fruit were infected with B. cinerea B05.10, and the fruit and fungal proteomes were identified concurrently 3 days postinfection. One hundred eighty-six tomato proteins were identified in common among red ripe and red ripe-equivalent ripening inhibited (rin) mutant tomato fruit infected by B. cinerea. However, the limited infections by B. cinerea of mature green wild type fruit resulted in 25 and 33% fewer defense-related tomato proteins than in red and rin fruit, respectively. In contrast, the ripening stage of genotype of the fruit infected did not affect the secreted proteomes of B. cinerea. The composition of the collected proteins populations and the putative functions of the identified proteins argue for their role in plant−pathogen interactions.

show abstract

“…After being centrifuged at 7000 × g and 4 °C for 15 min, the supernatant was collected for further enrichment. The exoenzymes induced by PNL or pectin in vitro were also prepared according to the methods 53 . Briefly, an active M. acerina disc (5 mm diameter) was grown in 100 mL of Czapek's Dox liquid medium.…”

Section: Extraction Of Extracellular Crude Enzymesmentioning

confidence: 99%

Discovery of plant chemical defence mediated by a two-component system involving β-glucosidase in Panax species

Ma,

Liu,

Guo

et al. 2024

Nat Commun

View full text Add to dashboard Cite

Plants usually produce defence metabolites in non-active forms to minimize the risk of harm to themselves and spatiotemporally activate these defence metabolites upon pathogen attack. This so-called two-component system plays a decisive role in the chemical defence of various plants. Here, we discovered that Panax notoginseng, a valuable medicinal plant, has evolved a two-component chemical defence system composed of a chloroplast-localized β-glucosidase, denominated PnGH1, and its substrates 20(S)-protopanaxadiol ginsenosides. The β-glucosidase and its substrates are spatially separated in cells under physiological conditions, and ginsenoside hydrolysis is therefore activated only upon chloroplast disruption, which is caused by the induced exoenzymes of pathogenic fungi upon exposure to plant leaves. This activation of PnGH1-mediated hydrolysis results in the production of a series of less-polar ginsenosides by selective hydrolysis of an outer glucose at the C-3 site, with a broader spectrum and more potent antifungal activity in vitro and in vivo than the precursor molecules. Furthermore, such β-glucosidase-mediated hydrolysis upon fungal infection was also found in the congeneric species P. quinquefolium and P. ginseng. Our findings reveal a two-component chemical defence system in Panax species and offer insights for developing botanical pesticides for disease management in Panax species.

show abstract

Expression of exo-polygalacturonases inBotrytis cinerea

Cited by 30 publications

References 16 publications

Characterization of an Exopolygalacturonase from Aspergillus niger

Characterization of an Exopolygalacturonase from Aspergillus niger

Proteomic Analysis of Ripening Tomato Fruit Infected by Botrytis cinerea

Discovery of plant chemical defence mediated by a two-component system involving β-glucosidase in Panax species

Contact Info

Product

Resources

About