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Published on December 1, 2006; 10.1104/pp.106.092635


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Received November 4, 2006
Accepted November 20, 2006

Conservation of the SOS Salt Tolerance Pathway in Rice

Juliana Martínez-Atienza , Xingyu Jiang , Blanca Garciadeblas , Imelda Mendoza , Jian-Kang Zhu , José M. Pardo *, and Francisco J. Quintero

Instituto de Recursos Naturales y Agrobiología. Consejo Superior de Investigaciones Científicas. Reina Mercedes, 10. Sevilla-41012. Spain
Departamento de Biotecnología, Escuela Técnica Superior de Ingenieros Agrónomos. Universidad Politécnica de Madrid. Madrid-28040. Spain
Department of Botany and Plant Sciences. Institute of Integrative Genome Biology. 2150 Batchelor Hall. University of California. Riverside, CA 92521

* Corresponding author; email: pardo{at}cica.es.

The salt tolerance of rice (Oryza sativa) correlates with the ability to exclude Na+ from the shoot and to maintain a low cellular Na+/K+ ratio. We have identified a rice plasma membrane Na+/H+ exchanger that, on the basis of genetic and biochemical criteria, is the functional homologue of the Arabidopsis thaliana SOS1 protein. The rice transporter, denoted by OsSOS1, demonstrated a capacity for Na+/H+ exchange in plasma membrane vesicles of yeast cells and reduced their net cellular Na+ content. The Arabidopsis protein kinase complex SOS2/SOS3, which positively controls the activity of AtSOS1, phosphorylated OsSOS1 and stimulated its activity in vivo and in vitro. Moreover, OsSOS1 suppressed the salt sensitivity of a sos1-1 mutant of Arabidopsis. These results represent the first molecular and biochemical characterization of a Na+ efflux protein from monocots. Putative rice homologues of the Arabidopsis protein kinase SOS2 and its Ca2+-dependent activator SOS3 were identified also. OsCIPK24 and OsCBL4 acted coordinately to activate OsSOS1 in yeast cells, and they could be exchanged with their Arabidopsis counterpart to form heterologous protein kinase modules that activated both OsSOS1 and AtSOS1 and that suppressed the salt sensitivity of sos2 and sos3 mutants of Arabidopsis. These results demonstrate that the SOS salt tolerance pathway operates in cereals and evidence a high degree of structural conservation among the SOS proteins from dicots and monocots.




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