Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-2-9
pubmed:abstractText
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 Na(+)/H(+) antiporter SOS1 to bring about sodium ion homeostasis and salt tolerance. Constitutively active alleles of SOS2 can be constructed in vitro by changing Thr(168) 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 Thr(168)-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.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-10455050, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-10717008, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-10725350, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-10725382, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-11006339, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-11115899, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-11402167, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-11479571, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-11572991, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-11606781, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-11698666, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-12034882, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-12070350, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-12221975, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-12226505, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-12469134, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-14504388, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-14570921, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-9154808, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-9418048, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-9525853, http://linkedlifedata.com/resource/pubmed/commentcorrection/14742879-9632394
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins, http://linkedlifedata.com/resource/pubmed/chemical/C-terminal binding protein, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/SOS1 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/SOS2 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/SOS3 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Chloride, http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Hydrogen Antiporter
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1040-4651
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
435-49
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
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.
pubmed:affiliation
Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't