Literature summary extracted from
Zhang, L.; Kars, I.; Essenstam, B.; Liebrand, T.W.; Wagemakers, L.; Elberse, J.; Tagkalaki, P.; Tjoitang, D.; van den Ackerveken, G.; van Kan, J.A.
Fungal endopolygalacturonases are recognized as microbe-associated molecular patterns by the Arabidopsis receptor-like protein 'resposiveness to Bortrytis polygalacturonases 1' (2014), Plant Physiol., 164, 352-364.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
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3.2.1.15 |
expression of 10xMyc-tagged isozyme BcPG3 in Nicotiana benthamiana, Arabidopsis thaliana protein RBPG1 and its homologues form with isozyme BcPG3 when co-expressed in Nicotiana benthamiana |
Botrytis cinerea |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
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3.2.1.15 |
Botrytis cinerea |
- |
isozymes BcPG2, BcPG3, BcPG4, and BcPG6 |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.2.1.15 |
endopolygalacturonase |
- |
Botrytis cinerea |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.2.1.15 |
physiological function |
infiltration of the enzyme into Arabidopsis thaliana induces a necrotic response mediated via recognition of the enzyme by resposiveness to Bortrytis polygalacturonases 1, RBPG1, a leucine-rich repeat receptor-like protein, AtRLP42, which acts as a microbe-associated molecular pattern receptor. Most sever effects occur in Arabidopsis thaliana accessions Col-0, Kas-1, and Kas-2, but not in accessions Br-0 and Est-0, but responsiveness is a dominant trait, detailed genetic analysis of accession responsiveness to the different isozymes, overview. RBPG1 homologues physically interact with isozyme BcPG3 and Arabidopsis leucine-rich repeat receptor-like protein, SOBIR1 |
Botrytis cinerea |