ArticleMolecular and cellular biochemistry2016
Expression and characterization of the SOS1 Arabidopsis salt tolerance protein.
Article in Molecular and cellular biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- Integrated proteomic, chemical forms, and distribution analysis reveals NaCl-mediated detoxification of cadmium in Suaeda salsa.Plant cell reports · 2025Article
- Coevolutionary Patterns in SOS1 and NHX1: Insights into Plant Ion Homeostasis Proteins.International journal of molecular sciences · 2025Article
- Characterization of Critical Amino Acids in the Transport and Selectivity of the Plant NaInternational journal of molecular sciences · 2025Article
- The translocation of a chloride channel from the Golgi to the plasma membrane helps plants adapt to salt stress.Nature communications · 2024Article
- BcWRKY1 confers salt sensitivity via inhibiting Reactive oxygen species scavenging.Plant molecular biology · 2022Article
- Article
- Phylogenetic Diversity and Physiological Roles of Plant Monovalent Cation/HFrontiers in plant science · 2020Review
- Article
- Structural and Functional Changes in the NaInternational journal of molecular sciences · 2019Review
- Mapping of novel salt tolerance QTL in an Excalibur × Kukri doubled haploid wheat population.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2018Article
- Genome of Paulownia (Paulownia fortunei) illuminates the related transcripts, miRNA and proteins for salt resistance.Scientific reports · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
SOS1 is the plasma membrane Na(+)/H(+) antiporter of Arabidopsis thaliana. It is responsible for the removal of intracellular sodium in exchange for an extracellular proton. SOS1 is composed of 1146 amino acids. Approximately 450 make the membrane domain, while the protein contains and a very large regulatory cytosolic domain of about 696 amino acids. Schizosaccharomyces pombe contains the salt tolerance Na(+)/H(+) antiporter proteins sod2. We examined the ability of SOS1 to rescue salt tolerance in S. pombe with a knockout of the sod2 gene (sod2::ura4). In addition, we characterized the importance of the regulatory tail of SOS1, in expression of the protein in S. pombe. We expressed full-length SOS1 and SOS1 shortened at the C-terminus and ending at amino acids 766 (medium) and 481 (short). The short version of SOS1 conveyed salt tolerance to sod2::ura4 yeast and Western blotting revealed that the protein was present. The protein was also targeted to the plasma membrane. The medium and full-length SOS1 protein were partially degraded and were not as well expressed as the short version of SOS1. The SOS1 short protein was also able to reduce Na(+) content in S. pombe. The full-length SOS1 dimerized and depended on the presence of the cytosolic tail. An analysis of SOS1 predicted a topology of 13 transmembrane segments, distinct from E. coli NhaA but similar to the Na(+)/H(+) exchangers Methanocaldococcus jannaschii NhaP1 and Thermus thermophile NapA.
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