This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Batelli, G.
Right arrow Articles by Zhu, J.-K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Batelli, G.
Right arrow Articles by Zhu, J.-K.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2007, p. 7781-7790, Vol. 27, No. 22
0270-7306/07/$08.00+0     doi:10.1128/MCB.00430-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

SOS2 Promotes Salt Tolerance in Part by Interacting with the Vacuolar H+-ATPase and Upregulating Its Transport Activity{triangledown}

Giorgia Batelli,1,2 Paul E. Verslues,1 Fernanda Agius,1 Quansheng Qiu,3,{dagger} Hiroaki Fujii,1 Songqin Pan,1 Karen S. Schumaker,3 Stefania Grillo,2 and Jian-Kang Zhu1*

Institute for Integrative Genome Biology and Department of Botany and Plant Sciences, University of California, Riverside, California 92521,1 CNR-IGV Institute of Plant Genetics and Department of Soil, Plant, Environmental and Animal Production Sciences, University of Naples Federico II, 80055 Portici, Italy,2 Department of Plant Sciences, University of Arizona, Tucson, Arizona 857213

Received 13 March 2007/ Returned for modification 23 May 2007/ Accepted 28 August 2007

The salt overly sensitive (SOS) pathway is critical for plant salt stress tolerance and has a key role in regulating ion transport under salt stress. To further investigate salt tolerance factors regulated by the SOS pathway, we expressed an N-terminal fusion of the improved tandem affinity purification tag to SOS2 (NTAP-SOS2) in sos2-2 mutant plants. Expression of NTAP-SOS2 rescued the salt tolerance defect of sos2-2 plants, indicating that the fusion protein was functional in vivo. Tandem affinity purification of NTAP-SOS2-containing protein complexes and subsequent liquid chromatography-tandem mass spectrometry analysis indicated that subunits A, B, C, E, and G of the peripheral cytoplasmic domain of the vacuolar H+-ATPase (V-ATPase) were present in a SOS2-containing protein complex. Parallel purification of samples from control and salt-stressed NTAP-SOS2/sos2-2 plants demonstrated that each of these V-ATPase subunits was more abundant in NTAP-SOS2 complexes isolated from salt-stressed plants, suggesting that the interaction may be enhanced by salt stress. Yeast two-hybrid analysis showed that SOS2 interacted directly with V-ATPase regulatory subunits B1 and B2. The importance of the SOS2 interaction with the V-ATPase was shown at the cellular level by reduced H+ transport activity of tonoplast vesicles isolated from sos2-2 cells relative to vesicles from wild-type cells. In addition, seedlings of the det3 mutant, which has reduced V-ATPase activity, were found to be severely salt sensitive. Our results suggest that regulation of V-ATPase activity is an additional key function of SOS2 in coordinating changes in ion transport during salt stress and in promoting salt tolerance.

* Corresponding author. Mailing address: Institute of Integrative Genome Biology and Department of Botany and Plant Sciences, University of California, Riverside, CA 92521. Phone: (951) 827-7117. Fax: (951) 827-7115. E-mail: jian-kang.zhu{at}ucr.edu

{triangledown} Published ahead of print on 17 September 2007.

{dagger} Present address: Department of Plant Biology, University of Illinois, Urbana, IL 61801.

Molecular and Cellular Biology, November 2007, p. 7781-7790, Vol. 27, No. 22
0270-7306/07/$08.00+0     doi:10.1128/MCB.00430-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lin, H., Yang, Y., Quan, R., Mendoza, I., Wu, Y., Du, W., Zhao, S., Schumaker, K. S., Pardo, J. M., Guo, Y. (2009). Phosphorylation of SOS3-LIKE CALCIUM BINDING PROTEIN8 by SOS2 Protein Kinase Stabilizes Their Protein Complex and Regulates Salt Tolerance in Arabidopsis. Plant Cell 21: 1607-1619 [Abstract] [Full Text]  
  • Queiros, F., Fontes, N., Silva, P., Almeida, D., Maeshima, M., Geros, H., Fidalgo, F. (2009). Activity of tonoplast proton pumps and Na+/H+ exchange in potato cell cultures is modulated by salt. J Exp Bot 60: 1363-1374 [Abstract] [Full Text]  
  • Minami, A., Fujiwara, M., Furuto, A., Fukao, Y., Yamashita, T., Kamo, M., Kawamura, Y., Uemura, M. (2009). Alterations in Detergent-Resistant Plasma Membrane Microdomains in Arabidopsis thaliana During Cold Acclimation. Plant Cell Physiol 50: 341-359 [Abstract] [Full Text]  
  • Fujii, H., Zhu, J.-K. (2009). An Autophosphorylation Site of the Protein Kinase SOS2 Is Important for Salt Tolerance in Arabidopsis. Mol Plant 0: ssn087v1-ssn087 [Abstract] [Full Text]  
  • Verslues, P. E., Batelli, G., Grillo, S., Agius, F., Kim, Y.-S., Zhu, J., Agarwal, M., Katiyar-Agarwal, S., Zhu, J.-K. (2007). Interaction of SOS2 with Nucleoside Diphosphate Kinase 2 and Catalases Reveals a Point of Connection between Salt Stress and H2O2 Signaling in Arabidopsis thaliana. Mol. Cell. Biol. 27: 7771-7780 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»