Abstract
The sos1 mutant of Arabidopsis thaliana is more than 20 times more sensitive to NaCl stress than wild type Arabidopsis. Because proline (Pro) is generally thought to have an important role in plant salt tolerance, the sos1 mutant and the wild type were compared with respect to their capacity to accumulate Pro under NaCl stress, and sos1 mutant plants accumulated more Pro than wild-type. The P5CS gene, which catalyzes the rate-limiting step in Pro biosynthesis, is induced by salt stress to a higher level in sos1 than in the wild type. Although a defective high-affinity K uptake system in sos1 causes K deficiency and inhibits growth in NaCl-treated plants, this decrease is not a sufficient signal for Pro accumulation and P5CS gene expression. Not all salt-stress-induced genes have a higher level of expression in sos1. The expression levels of AtPLC and RD29A, which encode a phospholipase C homolog and a putative protective protein, respectively, are the same in sos1 as in the wild type. However, the expression of AtMYB, which encodes a putative transcriptional factor, is induced to a much higher level by salt stress in sos1. Thus, the SOS1 gene product serves as a negative regulator for the expression of P5CS and AtMYB, but has no effect on AtPLC and RD29A expression.
MeSH Terms
1-Pyrroline-5-Carboxylate Dehydrogenase
Arabidopsis/drug effects,genetics,metabolism
DNA-Binding Proteins/biosynthesis
Gene Expression Regulation, Plant
Genes, Plant
Isoenzymes/biosynthesis
Mutation
Osmotic Pressure
Oxidoreductases Acting on CH-NH Group Donors/biosynthesis
Plant Proteins/biosynthesis
Potassium/pharmacology
Proline/biosynthesis
Sodium Chloride/pharmacology
Transcription Factors/biosynthesis
Type C Phospholipases/biosynthesis
Chemicals
DNA-Binding Proteins
Isoenzymes
Plant Proteins
Transcription Factors
Sodium Chloride
Proline
1-Pyrroline-5-Carboxylate Dehydrogenase
Oxidoreductases Acting on CH-NH Group Donors
Type C Phospholipases
Potassium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Liu J
Department of Plant Sciences, University of Arizona, Tucson 85721, USA.
Zhu J K
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