Literature summary for 3.2.1.15 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Botrytis cinerea	-	isozymes BcPG2, BcPG3, BcPG4, and BcPG6	-

Synonyms

Synonyms	Comment	Organism
endopolygalacturonase	-	Botrytis cinerea

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)