The plant wound hormone systemin binds with the N-terminal part to its receptor but needs the C-terminal part to activate it

111Citations
Citations of this article
45Readers
Mendeley users who have this article in their library.

Abstract

Suspension-cultured cells of Lycopersicon peruvianum respond with rapid medium alkalinization and a strong increase of a MAP kinase-like activity when treated with subnanomolar concentrations of the plant wound hormone systemin. Systemin fragments comprising the N-terminal 14 amino acids (syst1-14) or the C-terminal four amino acids (syst15-18), added singly or in combination, were inactive as inducers of these responses. Syst1-14 but not syst15-18 antagonized activity of intact systemin in a competitive manner. Likewise, intact systemin showed stimulatory, syst1-14 antagonistic activity, and syst15-18 showed no activity in leaf pieces of tomato (L. esculentum) plants assayed for the induction of ethylene biosynthesis. To study the molecular basis of perception, we extended the C-terminal end of systemin by a tyrosine residue and radio-iodinated it to yield systemin-125I-iodotyrosine. In membrane preparations of L. peruvianum, this radioligand exhibited rapid, saturable, and reversible binding to a single class of binding sites. Binding showed a dissociation constant of ~1 nM, and binding of radioligand was efficiently competed by unlabeled systemin but not by syst15-18 or structurally unrelated peptides. Binding was also competed by the systemin antagonists syst1-14 and syst-Ala-17 (IC50 of 500 and 1000 nM, respectively). Thus, this binding site exhibits the characteristics expected for a functional systemin receptor. Based on these results, we propose a two-step mechanism for systemin action, with binding of the N-terminal part to the receptor as the first step and activation of responses with the C-terminal part as the second step.

References Powered by Scopus

A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins

836Citations
N/AReaders
Get full text

Electrical signalling and systemic proteinase inhibitor induction in the wounded plant

405Citations
N/AReaders
Get full text

Structure, expression, and antisense inhibition of the systemin precursor gene

355Citations
N/AReaders
Get full text

Cited by Powered by Scopus

Perception of the Bacterial PAMP EF-Tu by the Receptor EFR Restricts Agrobacterium-Mediated Transformation

1485Citations
N/AReaders
Get full text

Plants have a sensitive perception system for the most conserved domain of bacterial flagellin

1260Citations
N/AReaders
Get full text

Wound signalling in plants

667Citations
N/AReaders
Get full text

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Cite

CITATION STYLE

APA

Meindl, T., Boller, T., & Felix, G. (1998). The plant wound hormone systemin binds with the N-terminal part to its receptor but needs the C-terminal part to activate it. Plant Cell, 10(9), 1561–1570. https://doi.org/10.1105/tpc.10.9.1561

Readers' Seniority

Tooltip

PhD / Post grad / Masters / Doc 18

49%

Professor / Associate Prof. 9

24%

Researcher 8

22%

Lecturer / Post doc 2

5%

Readers' Discipline

Tooltip

Agricultural and Biological Sciences 33

85%

Biochemistry, Genetics and Molecular Bi... 4

10%

Engineering 1

3%

Chemistry 1

3%

Save time finding and organizing research with Mendeley

Sign up for free