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First published online April 1, 2005; 10.1104/pp.104.058958

Plant Physiology 138:529-536 (2005)
© 2005 American Society of Plant Biologists

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PLANTS INTERACTING WITH OTHER ORGANISMS

Virus Induction of Heat Shock Protein 70 Reflects a General Response to Protein Accumulation in the Plant Cytosol1

Frederic Aparicio2, Carole L. Thomas, Carsten Lederer3, Yan Niu, Daowen Wang and Andrew J. Maule*

John Innes Centre, Norwich NR4 7UH, United Kingdom (F.A., C.L.T., C.L., A.J.M.); and Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China (Y.N., D.W.)

Different cytoplasmically replicating RNA viruses were shown to induce a specific subset of heat-inducible heat shock protein 70 (HSP70) genes in Arabidopsis (Arabidopsis thaliana). To identify the inducing principle, a promoter::reporter system was developed for the facile analysis of differentially responding Arabidopsis HSP70 genes, by infiltration into Nicotiana benthamiana leaves. Through transient expression of individual viral cistrons or through deletion analysis of a viral replicon, we were unable to identify a unique inducer of HSP70. However, there was a positive correlation between the translatability of the test construct and the differential induction of HSP70. Since these data implied a lack of specificity in the induction process, we also expressed a random series of cytosolically targeted Arabidopsis genes and showed that these also differentially induced HSP70. Through a comparison of different promoter::reporter constructs and through measurements of the steady-state levels of the individual proteins, it appeared that the HSP70 response reflected the ability of the cytosol to sense individual properties of particular proteins when expressed at high levels. This phenomenon is reminiscent of the unfolded protein response observed when the induced accumulation of proteins in the endoplasmic reticulum also induces a specific suite of chaperones.

1 This work was supported by a grant-in-aid from the Biotechnology and Biological Sciences Research Council, UK, to the John Innes Centre and by the National Natural Science Foundation of China (grant nos. 39725017 and 39670033). F.A. was a recipient of a Spanish Government Postdoctoral Fellowship. C.L. was supported by a John Innes Foundation Studentship. This work was carried out under licenses PHL 185A/4512 and PHL 185A/4513 issued by the UK Department of the Environment, Food and Rural Affairs.

2 Present address: Instituto de Biología Molecular y Celular de Plantas (UPV-CSIC), Avenida de los Naranjos s/n, 46022 Valencia, Spain.

3 Present address: Molecular Biology and Biochemistry Laboratory, University of Cyprus, Kallipoleos Avenue 75, 1678 Nicosia, Cyprus.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.058958.

* Corresponding author; e-mail andy.maule{at}bbsrc.ac.uk; fax 44–1603–450045.

Received December 29, 2004; returned for revision February 3, 2005; accepted February 3, 2005.




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