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SOS1 tonoplast neo-localization and the RGG protein SALTY are important in the extreme salinity tolerance of Salicornia bigelovii
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SYSNO ASEP 0599179 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title SOS1 tonoplast neo-localization and the RGG protein SALTY are important in the extreme salinity tolerance of Salicornia bigelovii Author(s) Salazar, O. R. (SA)
Chen, K. (CN)
Melino, V. J. (SA)
Reddy, M. P. (SA)
Hřibová, Eva (UEB-Q) RID, ORCID
Čížková, Jana (UEB-Q) RID, ORCID
Beránková, Denisa (UEB-Q) ORCID
Vega, J. P. A. (SA)
Leal, L. M. C. (SA)
Aranda, M. (SA)
Jaremko, Ł. (SA)
Jaremko, M. (SA)
Fedoroff, N. V. (US)
Tester, M. (SA)
Schmoeckel, S. M. (DE)Number of authors 15 Article number 4279 Source Title Nature Communications. - : Nature Publishing Group - ISSN 2041-1723
Roč. 15, č. 1 (2024)Number of pages 21 s. Language eng - English Country US - United States Keywords multiple sequence alignment ; na+/h+ exchange activity ; plasma-membrane ; arabidopsis-thaliana ; proteomics data ; endoplasmic-reticulum ; increased vacuolar ; phase-separation ; genome sequence ; gene ontology OECD category Cell biology Method of publishing Open access Institutional support UEB-Q - RVO:61389030 UT WOS 001228176400004 EID SCOPUS 85193752724 DOI https://doi.org/10.1038/s41467-024-48595-5 Annotation The identification of genes involved in salinity tolerance has primarily focused on model plants and crops. However, plants naturally adapted to highly saline environments offer valuable insights into tolerance to extreme salinity. Salicornia plants grow in coastal salt marshes, stimulated by NaCl. To understand this tolerance, we generated genome sequences of two Salicornia species and analyzed the transcriptomic and proteomic responses of Salicornia bigelovii to NaCl. Subcellular membrane proteomes reveal that SbiSOS1, a homolog of the well-known SALT-OVERLY-SENSITIVE 1 (SOS1) protein, appears to localize to the tonoplast, consistent with subcellular localization assays in tobacco. This neo-localized protein can pump Na+ into the vacuole, preventing toxicity in the cytosol. We further identify 11 proteins of interest, of which SbiSALTY, substantially improves yeast growth on saline media. Structural characterization using NMR identified it as an intrinsically disordered protein, localizing to the endoplasmic reticulum in planta, where it can interact with ribosomes and RNA, stabilizing or protecting them during salt stress. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2025 Electronic address https://doi.org/10.1038/s41467-024-48595-5
Number of the records: 1