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Isolation and characterization of the proteinase inhibitor-inducing factor from tomato leaves. Identity and activity of poly- and oligogalacturonide fragments. by P D Bishop; G Pearce; J E Bryant; C A Ryan is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Mild acid hydrolysis of a small (M. = 6 kDa) pectic polysaccharide isolated from tomato leaves, an inducer of the synthesis and accumulation of two proteinase inhibitors in excised tomato plants, yielded a a-Dpolygalacturonic acid polymer with degree of polymerization = 20 that retained proteinase inhibitor-inducing activity. Enzymic and acid hydrolysis of this polygalacturonan yielded a series of a-1,'i-D-galacturonic acid oligomers with degrees of polymerization from 2 to 6 which were purified to homogeneity and assayed for proteinase inhibitor-inducing activity in young excised tomato plants. All of the oligomers exhibited activity. The hexagalacturonide possessed the highest activity and the trimer the lowest. The evidence supports a possible role for plant cell wall fragments as systemic messengers that regulate the expression of proteinase inhibitor genes in plant leaves in response to pest attacks.

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Author

P D Bishop; G Pearce; J E Bryant; C A Ryan

Publisher

Elsevier BV

Published

1984

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)