Induction of Electrolyte Loss, Tissue Maceration, and Cellular Death of Potato Tissue by an Endopolygalacturonate Trans-Eliminase

Mount, Mark S.

doi:10.1094/phyto-60-924

Cited by 132 publications

(50 citation statements)

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“…Purified Erwinia pectic enzymes macerate plant tissue and cause plant cell death (2,23), and cloned Erwinia pectic enzyme genes confer the ability to macerate plant tissue on the non-plant pathogen E. coli (7,15,27,31). Biochemical and genetic data (5) indicate that the excreted Erwinia enzymes pectate lyase, polygalacturonase, and pectin methylesterase act in a concerted manner to degrade the pectic portion of plant cell walls and provide nutrition for the pathogen.…”

mentioning

confidence: 99%

Analysis of the Pseudomonas solanacearum polygalacturonase encoded by pglA and its involvement in phytopathogenicity

1988

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A major endopolygalacturonase excreted by Pseudomonas solanacearum was purified to >95 % homogeneity and shown to have an isoelectric point of 9.0 and a subunit molecular mass of 52 kilodaltons (kDa). The gene encoding this enzyme (pglA) was isolated from a genomic library of P. solanacearum DNA based on its expression in Escherichia coli and shown to be contained on a 1.8-kilobase DNA fragment. The identity of the pglA gene product and the 52-kDa polygalacturonase was demonstrated by immunoadsorption and isoelectric focusing experiments. The cloned pglA gene was apparently expressed from its own promoter in E. coli and its product was partially secreted into the periplasm. The pglA gene was insertionally inactivated in vitro and used to mutate the chromosomal pgL4 gene of P. solanacearum by marker exchange mutagenesis. The resulting mutant strain was deficient in production of the 52-kDa polygalacturonase and took twice as long to wilt and kill tomato plants as the wild-type parent in plant bioassay experiments. Complementation in trans with the wild-type cloned pg4 gene restored virulence to near wild-type levels. The data indicate that the pglA gene is important, but not absolutely necessary, for pathogenesis.

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confidence: 99%

Analysis of the Pseudomonas solanacearum polygalacturonase encoded by pglA and its involvement in phytopathogenicity

1988

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“…Of these enzymes, those that degrade pectin are believed to be of key importance in pathogenesis. The pectic-degrading enzymes secreted by a number of pathogens cause maceration of plant tissue, loss in electrolytes, and cell death (4,6,10,14). Also, pectic-degrading enzymes have been detected in lesion areas of infected plant tissue (2,5,9,15).…”

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Host-Pathogen Interactions

Fisher¹,

Anderson²,

Albersheim³

1973

Plant Physiol.

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“…That polygalacturonic acid-degrading enzymes are able to attack some plant cell components. although not necessarily cell walls, has been established by demonstrating that purified preparations of such enzymes can initiate cell killing (10,15).…”

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confidence: 99%

A Cell Wall-degrading Endopolygalacturonase Secreted by Colletotrichum lindemuthianum

et al. 1972

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Cultures of Colletotrichum lindertmuthianum (Saccardo and Magnus) Scribner have been induced to secrete an endopolygalacturonase (polygalacturonide glyeanohydrolase EC3.2. 1.15). This enzyme has been brought to a high state of purity bv ion exchange, gel filtration, and agarose affinity chromatography. The enzyme has optimal activity at pH 5, has an apparent molecular weight as determined bv gel filtration of about 70,000, and prefers polygalacturonic acid to pectin as its substrate. The enzymne, while hydrolyzing only 1% of the glycosidic bonds, reduces the viscosity of a polygalacturonic solution by 50 %. Nevertheless, the initial as well as the final products of polygalacturonic acid hydrolysis are predominantly tri-and digalacturonic acid and, to a lesser extent, monogalacturonic acid. The purified enzyme catalyzes the removal of about 80% of the galacturonic acid residues of cell walls isolated from suspension-cultured sycamore cells (Acer pseudoplatanus) as well as from the walls isolated from 8-day-old Red Kidney bean (Phaseolus vulgaris) hypocotvls.Most polysaccharide-degrading enzymes are unable to attack effectively their substrates within isolated cell walls. Evidence has been presented which suggests that the "wall-modifying enzyme" purified from the culture filtrate of Aspergillus niger is a polygalacturonic acid-degrading enzyme (13). Treatment of walls with the wall-modifying enzyme permits other enzymes to degrade their substrates within the wall. Additional evidence that polygalacturonic acid-degrading enzymes are probably able, without assistance, to degrade cell walls comes from numerous efforts to demonstrate that these enzymes macerate plant tissues (2,4,5,7,12,18,20

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Induction of Electrolyte Loss, Tissue Maceration, and Cellular Death of Potato Tissue by an Endopolygalacturonate Trans-Eliminase

Cited by 132 publications

References 0 publications

Analysis of the Pseudomonas solanacearum polygalacturonase encoded by pglA and its involvement in phytopathogenicity

Analysis of the Pseudomonas solanacearum polygalacturonase encoded by pglA and its involvement in phytopathogenicity

Host-Pathogen Interactions

A Cell Wall-degrading Endopolygalacturonase Secreted by Colletotrichum lindemuthianum

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