| dc.contributor |
National Institutes of Health (US) |
|
| dc.contributor |
Department of Energy (US) |
|
| dc.contributor |
Ministerio de Ciencia y Tecnología (España) |
|
| dc.contributor |
Junta de Andalucía |
|
| dc.creator |
Guo, Yan |
|
| dc.creator |
Qiu, Quan-Sheng |
|
| dc.creator |
Quintero, Francisco J. |
|
| dc.creator |
Pardo, José M. |
|
| dc.creator |
Ohta, Masaru |
|
| dc.creator |
Zhang, Changqing |
|
| dc.creator |
Schumaker, Karen S. |
|
| dc.creator |
Jian-Kang, Zhu |
|
| dc.date |
2008-03-27T13:34:15Z |
|
| dc.date |
2008-03-27T13:34:15Z |
|
| dc.date |
2006-07-27 |
|
| dc.date.accessioned |
2017-01-31T01:01:13Z |
|
| dc.date.available |
2017-01-31T01:01:13Z |
|
| dc.identifier |
Plant Cell 16(2): 435–449 (2004). |
|
| dc.identifier |
1040-4651 |
|
| dc.identifier |
http://hdl.handle.net/10261/3339 |
|
| dc.identifier |
10.1105/tpc.019174 |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3339 |
|
| dc.description |
Fecha de solicitud: 24-01-2006.- Titulares: Consejo Superior de Investigaciones Científicas (CSIC).- The
Arizona Board of Regents on Behalf
of the University of Arizona. |
|
| dc.description |
In Arabidopsis thaliana, the calcium binding protein Salt Overly Sensitive3 (SOS3) interacts with and activates the protein
kinase SOS2, which in turn activates the plasma membrane Na1/H1 antiporter SOS1 to bring about sodium ion homeostasis
and salt tolerance. Constitutively active alleles of SOS2 can be constructed in vitro by changing Thr168 to Asp in the
activation loop of the kinase catalytic domain and/or by removing the autoinhibitory FISL motif from the C-terminal
regulatory domain. We expressed various activated forms of SOS2 in Saccharomyces cerevisiae (yeast) and in A. thaliana
and evaluated the salt tolerance of the transgenic organisms. Experiments in which the activated SOS2 alleles were
coexpressed with SOS1 in S. cerevisiae showed that the kinase activity of SOS2 is partially sufficient for SOS1 activation in
vivo, and higher kinase activity leads to greater SOS1 activation. Coexpression of SOS3 with SOS2 forms that retained the
FISL motif resulted in more dramatic increases in salt tolerance. In planta assays showed that the Thr168-to-Asp–activated
mutant SOS2 partially rescued the salt hypersensitivity in sos2 and sos3 mutant plants. By contrast, SOS2 lacking only the
FISL domain suppressed the sos2 but not the sos3 mutation, whereas truncated forms in which the C terminus had been
removed could not restore the growth of either sos2 or sos3 plants. Expression of some of the activated SOS2 proteins in
wild-type A. thaliana conferred increased salt tolerance. These studies demonstrate that the protein kinase activity of SOS2
is partially sufficient for activation of SOS1 and for salt tolerance in vivo and in planta and that the kinase activity of SOS2 is
limiting for plant salt tolerance. The results also reveal an essential in planta role for the SOS2 C-terminal regulatory domain
in salt tolerance. |
|
| dc.description |
This work was supported by National Institutes of Health Grant
R01GM59138 to J.-K.Z., U.S. Department of Energy Grant DE-FG03-
93ER20120 to K.S.S., and the Southwest Consortium on Plant Genetics
and Water Resources to J.-K.Z. and K.S.S. F.J.Q. and J.M.P. were
supported by Grant BIO2000-0398 from the Spanish Ministry of Science
and Technology and Grant CVI-148 from Junta de Andalucía. |
|
| dc.description |
Peer reviewed |
|
| dc.format |
940002 bytes |
|
| dc.format |
application/pdf |
|
| dc.language |
eng |
|
| dc.publisher |
American Society of Plant Biologists |
|
| dc.rights |
closedAccess |
|
| dc.title |
Transgenic evaluation of activated mutant alleles of SOS2 reveals a critical requirement for its kinase activity and C-terminal regulatory domain for salt tolerance in Arabidopsis thaliana. |
|
| dc.type |
Artículo |
|