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First published online October 10, 2008; 10.1105/tpc.108.201011 The Plant Cell 20:2542
OTS1/2-Dependent DeSUMOylation Boosts Salt ToleranceScience Editor kfarquharson{at}aspb.org
Dubbed "ubiquitin's mysterious cousin" (Müller et al., 2001 Conti et al. (pages 2894–2908) provide evidence that two SUMO proteases, OVERLY TOLERANT TO SALT1 (OTS1) and OTS2, act redundantly to regulate the salt stress response in Arabidopsis. In a loss-of-function analysis using T-DNA insertion knockouts, the authors demonstrated that the ots1 ots2 double mutant is hypersensitive to salt, whereas the ots1 and ots2 single mutants exhibit the same degree of salt-dependent reduction in root growth as the wild type. Immunoblot analysis of proteins isolated from wild-type Arabidopsis seedlings exposed to a range of salt concentrations revealed a dose-dependent increase in SUMOylation of cellular proteins. Although both the single (ots1 or ots2) and double (ots1 ots2) mutants had higher levels of SUMOylated proteins than the wild type under normal growth conditions, only the double mutant had unusually high levels of SUMOylation when exposed to salt stress. At high salinity, plants overexpressing OTS1 (see figure ) faired much better than both wild-type plants and plants ectopically expressing the active site mutant ots1 (C526S) and had reduced levels of SUMOylated proteins. Thus, OTS1 protease activity appears to impart salt tolerance by reducing levels of SUMOylation.
Next, the scientists investigated the effect of salt stress on SUMO protease levels. While salinity did not affect mRNA levels of OTS1, protein levels of TAP-tagged OTS1 constitutively expressed in an ots1 background rapidly declined in the presence of salt. Preincubation with proteasome inhibitor prevented loss of OTS1 during salt stress. The authors propose that the natural salt sensitivity seen in Arabidopsis is partially due to the accumulation of SUMO conjugates that occurs when OTS1 and OTS2 proteases are degraded.
Finally, GFP-tagged OTS1 and YFP-tagged OTS2 were both shown to localize to the nucleus when transiently expressed in tobacco cells. Interestingly, most SUMO substrates in animals, yeast, and plants also localize to the nucleus (Novatchkova et al., 2004 Footnotes www.plantcell.org/cgi/doi/10.1105/tpc.108.201011 REFERENCES Conti, L., Price, G., O'Donnell, E., Schwessinger, B., Dominy, P., and Sadanandom, A. (2008). Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and -2 regulate salt stress responses in Arabidopsis. Plant Cell 20: 2894–2908. Kurepa, J., Walker, J.M., Smalle, J., Gosink, M.M., Davis, S.J., Durham, T.L., Sung, D.-Y., and Vierstra, R.D. (2003). The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. J. Biol. Chem. 278: 6862–6872. Müller, S., Hoege, C., Pyrowolakis, G., and Jentsch, S. (2001). Sumo, ubiquitin's mysterious cousin. Nat. Rev. Mol. Cell Biol. 2: 202–210.[CrossRef][Web of Science][Medline] Novatchkova, M., Budhiraja, R., Coupland, G., Eisenhaber, F., and Bachmair, A. (2004). SUMO conjugation in plants. Planta 220: 1–8.[CrossRef][Web of Science][Medline] Related articles in Plant Cell:
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