SENSITIVE TO FREEZING2 Aides in Resilience to Salt and Drought in Freezing-Sensitive Tomato.
SENSITIVE TO FREEZING2 (SFR2) is crucial for protecting chloroplast membranes following freezing in Arabidopsis (Arabidopsis thaliana). It has been shown that SFR2 homologs are present in all land plants, including freezing-sensitive species, raising the question of SFR2 function beyond freezing tolerance. Similar to freezing, salt and drought can cause dehydration. Thus, it is hypothesized that in freezing-sensitive plants SFR2 may play roles in their resilience to salt or drought. To test this hypothesis, SlSFR2 RNAi lines were generated in the cold/freezing-sensitive species tomato (Solanum lycopersicum [M82 cv]). Hypersensitivity to salt and drought of SlSFR2-RNAi lines was observed. Higher tolerance of wild-type tomatoes was correlated with the production of trigalactosyldiacylglycerol, a product of SFR2 activity. Tomato SFR2 in vitro activity is Mg2+-dependent and its optimal pH is 7.5, similar to that of Arabidopsis SFR2, but the specific activity of tomato SFR2 in vitro is almost double that of Arabidopsis SFR2. When salt and drought stress were applied to Arabidopsis, no conditions could be identified at which SFR2 was induced prior to irreversibly impacting plant growth, suggesting that SFR2 protects Arabidopsis primarily against freezing. Discovery of tomato SFR2 function in drought and salt resilience provides further insights into general membrane lipid remodeling-based stress tolerance mechanisms and together with protection against freezing in freezing-resistant plants such as Arabidopsis, it adds lipid remodeling as a possible target for the engineering of abiotic stress-resilient crops.
Department of Biochemistry and Molecular Biology (K.W., H.L.H., C.B.) and Department of Plant Biology (C.B.), Michigan State University, East Lansing, Michigan 48824; and.|MSU-Department of Energy Plant Research Laboratory, East Lansing, Michigan 48824 (K.W., H.L.H., C.B.).
Kun
0000-0003-1715-990X
K
Wang
Department of Biochemistry and Molecular Biology (K.W., H.L.H., C.B.) and Department of Plant Biology (C.B.), Michigan State University, East Lansing, Michigan 48824; and.|MSU-Department of Energy Plant Research Laboratory, East Lansing, Michigan 48824 (K.W., H.L.H., C.B.).
Hope Lynn
HL
Hersh
Department of Biochemistry and Molecular Biology (K.W., H.L.H., C.B.) and Department of Plant Biology (C.B.), Michigan State University, East Lansing, Michigan 48824; and benning@msu.edu.|MSU-Department of Energy Plant Research Laboratory, East Lansing, Michigan 48824 (K.W., H.L.H., C.B.) benning@msu.edu.
Christoph
0000-0001-8585-3667
C
Benning
D017360:Arabidopsis / Q000187:drug effects / Q000502:physiology; D029681:Arabidopsis Proteins / Q000378:metabolism; D002734:Chlorophyll / Q000378:metabolism; D055864:Droughts; D005615:Freezing; D018551:Solanum lycopersicum / Q000187:drug effects / Q000502:physiology*; D009154:Mutation / Q000235:genetics; D018515:Plant Leaves / Q000187:drug effects / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D030821:Plants, Genetically Modified; D034622:RNA Interference; D017386:Sequence Homology, Amino Acid; D012965:Sodium Chloride / Q000494:pharmacology*; D013312:Stress, Physiological / Q000187:drug effects; D001617:beta-Glucosidase / Q000378:metabolism
D029681:Arabidopsis Proteins; D010940:Plant Proteins; D002734:Chlorophyll; D012965:Sodium Chloride; C492903:SFR2 protein, Arabidopsis; D001617:beta-Glucosidase