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Planta

, Volume 219, Issue 3, pp 412–419 | Cite as

Import of polyphenol oxidase by chloroplasts is enhanced by methyl jasmonate

  • Shai Koussevitzky
  • Emma Ne’eman
  • Eitan Harel
Original Article

Abstract

Polyphenol oxidase (PPO; EC 1.10.3.2 or EC 1.14.18.1) takes part in the response of tomato plants (Lycopersicon esculentum Mill.) to wounding and herbivore attack, mediated by the octadecanoid wound-signaling pathway. Wounding and methyl jasmonate (MeJA) induce expression of ppo genes and markedly increase the level of the enzyme. We report that pretreatment with MeJA also markedly increased the ability of isolated tomato chloroplasts to import and process PPO precursors (pPPO). Pea (Pisum sativum L.) chloroplasts showed no such response. Wounding or ethylene alone was ineffective but ethylene was synergistic with MeJA. Treatment with MeJA conferred a strong binding of pPPO, or its processing intermediate, to thylakoids and subsequent translocation into the lumen and processing to the mature protein. The effect on PPO import and translocation was evident after 8–16 h exposure to MeJA. Membrane-bound pPPO was cross-linked to a proteinaceous component of the thylakoid translocation apparatus, apparently induced by MeJA. The import and processing of other nuclear-encoded thylakoid proteins were not affected by MeJA in tomato. A 90-kDa protein that co-fractionated with thylakoids was induced along with the increase in competence for PPO import, and was identified as the proteinase-inhibitor multicystatin. It is concluded that the 90-kDa protein observed is part of the MeJA-induced defense response of tomato, not a component of the thylakoid translocation apparatus.

Keywords

Chloroplast import Jasmonic acid Lycopersicon Multicystatin Polyphenol oxidase Thylakoid translocation 

Abbreviations

Chl

Chlorophyll

‘i’ and ‘p’

Prefixes used to denote the intermediate and precursor forms of a protein, respectively

JA

Jasmonic acid

LSU

Large subunit of Rubisco

MeJA

Methyl jasmonate

OE23 and OE33

23- and 33-kDa subunits of the oxygen-evolving complex of PSII

PC

Plastocyanin

pPPO (iPPO, PPO)

Precursor (intermediate, mature) form of polyphenol oxidase

Notes

Acknowledgements

This research was supported by grant US 2474-95C from The United States–Israel Binational Agricultural Research and Development Fund. We are extremely grateful to John C. Steffens, formerly of Cornell University, (Ithaca, NY) for providing the cloned ppo genes, and many helpful discussions. We thank Arieh Admon, the Protein Research Center, the Technion (Haifa, Israel) for protein sequencing, Abdussalam Azem, Biochemistry Department, Tel Aviv University (Tel Aviv, Israel) and Sophie Diamant, Department of Plant Sciences, The Hebrew University (Jerusalem, Israel) for help in the cross-linking experiments. We are grateful to Kunhua Chen, Todd Mockler and Todd Michael, Plant Biology laboratory, the Salk Institute (La Jolla, CA) for fruitful discussions and criticism.

This work is dedicated to Eitan Harel (1936–2003), a mentor and friend.

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Copyright information

© Springer-Verlag 2004

Authors and Affiliations

  • Shai Koussevitzky
    • 1
    • 2
  • Emma Ne’eman
    • 1
  • Eitan Harel
    • 1
  1. 1.Department of Plant SciencesThe Hebrew UniversityJerusalemIsrael
  2. 2.Plant Biology LaboratoryThe Salk Institute for Biological StudiesLa JollaUSA

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