Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Published on October 13, 2006; 10.1104/pp.106.088831

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Received August 25, 2006
Accepted October 4, 2006

SIZ1 SUMO E3 Ligase Facilitates Basal Thermotolerance in Arabidopsis Independent of Salicylic Acid

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, 625 Agriculture Mall Drive, Purdue University, West Lafayette, IN 47907
Division of Applied Life Science (BK21 program) and Environmental Biotechnology National Core Research Center, Graduate School of Gyeongsang National University, Jinju 660-701, Korea

* Corresponding author; email: paul.m.hasegawa.1{at}purdue.edu.

SUMO (small ubiquitin modifier) conjugation/deconjugation to heat shock transcription factors regulates DNA binding of the peptides and activation of heat shock protein (HSP) gene expression that modulates thermal adaptation in metazoans. AtSIZ1 is a SUMO E3 ligase that facilitates SUMO conjugation to substrate target proteins (sumoylation) in Arabidopsis (Arabidopsis thaliana). siz1 T-DNA mutations (siz1-2 and siz1-3; Miura et al., 2005) cause basal, but not acquired, thermosensitivity that occurs in conjunction with hyper-accumulation 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 HSPs, ascorbate peroxidase (APX)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.




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