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First published online October 13, 2006; 10.1104/pp.106.088831

Plant Physiology 142:1548-1558 (2006)
© 2006 American Society of Plant Biologists

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ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS

SIZ1 Small Ubiquitin-Like Modifier E3 Ligase Facilitates Basal Thermotolerance in Arabidopsis Independent of Salicylic Acid1,[W],[OA]

Chan Yul Yoo, Kenji Miura, Jing Bo Jin, Jiyoung Lee, Hyeong Cheol Park, David E. Salt, Dae-Jin Yun, Ray A. Bressan and Paul M. Hasegawa*

Center for Plant Environmental Stress Physiology, Purdue University, West Lafayette, Indiana 47907 (C.Y.Y., K.M., J.B.J., H.C.P., D.E.S., R.A.B., P.M.H.); and Division of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, and Environmental Biotechnology National Core Research Center, Graduate School of Gyeongsang National University, Jinju 660–701, Korea (J.L., D.-J.Y.)

Small ubiquitin-like modifier (SUMO) conjugation/deconjugation to heat shock transcription factors regulates DNA binding of the peptides and activation of heat shock protein gene expression that modulates thermal adaptation in metazoans. SIZ1 is a SUMO E3 ligase that facilitates SUMO conjugation to substrate target proteins (sumoylation) in Arabidopsis (Arabidopsis thaliana). siz1 T-DNA insertional mutations (siz1-2 and siz1-3; Miura et al., 2005) cause basal, but not acquired, thermosensitivity that occurs in conjunction with hyperaccumulation of salicylic acid (SA). NahG encodes a salicylate hydroxylase, and expression in siz1-2 seedlings reduces endogenous SA accumulation to that of wild-type levels and further increases thermosensitivity. High temperature induces SUMO1/2 conjugation to peptides in wild type but to a substantially lesser degree in siz1 mutants. However, heat shock-induced expression of genes, including heat shock proteins, ascorbate peroxidase 1 and 2, is similar in siz1 and wild-type seedlings. Together, these results indicate that SIZ1 and, by inference, sumoylation facilitate basal thermotolerance through processes that are SA independent.


1 This work was supported by the National Science Foundation Plant Genome Award (DBI–98–13360), by the Basic Science Project of Korea Science and Engineering Foundation (grant no. RO1–2006–000–10123–0 and postdoctoral fellowship to H.C.P.), by the Environmental Biotechnology National Core Research Center Project of Korea Science and Engineering Foundation (grant no. R15–2003–012–01002–00), and by the Biogreen 21 Program of the Rural Development Administration, Korea. This work is Purdue University Agricultural Research Program Paper 2006–17918.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Paul M. Hasegawa (paul.m.hasegawa.1{at}purdue.edu).

[W] The online version of this article contains Web-only data.

[OA] Open Access articles can be viewed online without a subscription.

www.plantphysiol.org/cgi/doi/10.1104/pp.106.088831

* Corresponding author; e-mail paul.m.hasegawa.1{at}purdue.edu; fax 765–494–0391.

Received August 25, 2006; accepted October 4, 2006; published October 13, 2006.




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