SULTR1;2 (Sulfate Transporter 1;2) is a high-affinity sulfate transporter in Arabidopsis thaliana responsible for sulfate uptake in roots under sulfur-deficient conditions . The SULTR1;2 antibody is a specialized tool designed to detect and quantify this transporter protein in plant tissues, enabling researchers to study its expression patterns, localization, and regulatory mechanisms .
Protein Localization: Used in immunofluorescence and confocal microscopy to confirm root-specific expression of SULTR1;2 .
Western Blot Analysis: Detects SULTR1;2 protein accumulation under varying sulfur conditions (e.g., 1,500 µM vs. 5 µM sulfate) .
Mutant Phenotype Validation: Validates loss-of-function mutants (e.g., sultr1;2 knockout lines) by confirming reduced or absent protein levels .
Posttranscriptional Regulation Studies: Tracks protein stability and degradation kinetics under sulfur-replete or sulfur-deprived conditions .
SULTR1;2 is critical for sulfate acquisition under low-sulfur conditions, with its protein levels increasing 8–72 hours after sulfur starvation .
Double knockout mutants (sultr1;1 sultr1;2) lack sulfate uptake activity, confirming functional redundancy with SULTR1;1 .
| Condition | SULTR1;2 mRNA Level | SULTR1;2 Protein Level |
|---|---|---|
| Sulfur-sufficient | Low | Undetectable |
| Sulfur-deficient | Moderately induced | Significantly increased |
Protein accumulation occurs independently of transcript levels, highlighting posttranscriptional control .
sultr1;2 mutants exhibit aberrant expression of sulfur-deficiency-responsive genes (e.g., BGLU28, SDI1), suggesting SULTR1;2 may act as a sulfur sensor .
Glutathione (GSH) accumulation correlates with SULTR1;2 protein levels, linking sulfate transport to cellular redox homeostasis .
Transgenic lines expressing epitope-tagged SULTR1;2 (e.g., SULTR1;2mycHis) rescued sultr1;2 mutant phenotypes, confirmed via anti-myc western blotting .
GFP-tagged SULTR1;2 lines showed root-specific fluorescence under sulfur deficiency, validated by fluorescence microscopy .
SLIM1 transcription factor regulates SULTR1;2 expression. Truncation of SLIM1’s C-terminal 57 amino acids abolished SULTR1;2 induction under sulfur deficiency .
Antibody Specificity: Validated using sultr1;2 knockout mutants, which show no detectable signal in western blots .
Cross-Reactivity: No cross-reactivity reported with other SULTR family members (e.g., SULTR1;1 or SULTR2;1) .
Quantitative Limits: Sensitivity thresholds require optimization for low-abundance protein detection in sulfur-sufficient conditions .
SULTR1;2 Function and Related Research:
Sulfur status: SULTR1;2 mRNA and protein levels increase under sulfur deficiency (5 µM sulfate) but remain detectable under sufficient sulfate (1,500 µM) .
Metabolite feedback: Glutathione (GSH) suppresses SULTR1;2 expression, while O-acetylserine (OAS) enhances it .
| Treatment | Sulfate (µM) | GSH (nmol/g FW) | SULTR1;2 mRNA (Relative) |
|---|---|---|---|
| Sulfur-sufficient | 1,500 | 120 | 1.0 (baseline) |
| Sulfur-deficient | 5 | 110 | 9.0 |
Context: SULTR1;2 mutants (sel1-15, sel1-16) show disrupted sulfate transport but retain aberrant sulfur-responsive gene expression (e.g., BGLU28 upregulation) even under high sulfate .
Approach:
Use immunofluorescence or confocal microscopy (as in ) to confirm plasma membrane localization.
Pair antibody-based protein quantification with sulfate uptake assays in mutants.
Check for post-translational modifications (e.g., interaction with OASTL ) that may decouple protein abundance from activity.
Co-immunoprecipitation (Co-IP): Identify binding partners like O-acetylserine(thiol)lyase (OASTL), which interacts with SULTR1;2’s STAS domain under OAS-rich conditions .
Protocol:
Use root microsomal fractions for membrane protein extraction.
Include sultr1;2 mutants as negative controls.
Functional validation: Test if OASTL binding alters sulfate uptake kinetics in heterologous systems (e.g., yeast ).
Experimental design:
Key finding: SULTR1;2 protein persists longer than mRNA after sulfate resupply, suggesting post-transcriptional stabilization .