ArticleThe Journal of membrane biology2013
Functional characterization of SdcF from Bacillus licheniformis, a homolog of the SLC13 Na⁺/dicarboxylate transporters.
Article in The Journal of membrane biology, 2013. 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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11 citing papers in PubMed, 12 citations in OpenAlex.
- Structures of the human sodium-citrate cotransporter NaCT with and without substrates.Structure (London, England : 1993) · 2026Article
- Structures of the human sodium-citrate cotransporter NaCT with and without substrates.bioRxiv : the preprint server for biology · 2026Article
- Structural insights into pink-eyed dilution protein (Oca2).Bioscience reports · 2023Article
- Membrane-anchored substrate binding proteins are deployed in secondary TAXI transporters.Biological chemistry · 2023Article
- Structural basis of ion - substrate coupling in the NaNature communications · 2022Article
- The ups and downs of elevator-type di-/tricarboxylate membrane transporters.The FEBS journal · 2022Article
- Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY.The Biochemical journal · 2021Article
- Article
- Transcriptional Regulation of the Outer Membrane Porin Gene ompW Reveals its Physiological Role during the Transition from the Aerobic to the Anaerobic Lifestyle of Escherichia coli.Frontiers in microbiology · 2016Article
- Genetic analysis of the assimilation of C5-dicarboxylic acids in Pseudomonas aeruginosa PAO1.Journal of bacteriology · 2014Article
- Functional characterization of a Na+-dependent dicarboxylate transporter from Vibrio cholerae.The Journal of general physiology · 2014Article
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3 authors at 2 institutions in 1 country.
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Abstract
The SdcF transporter from Bacillus licheniformis (gene BL02343) is a member of the divalent anion sodium symporter (DASS)/SLC13 family that includes Na⁺/dicarboxylate transporters from bacteria to humans. SdcF was functionally expressed in Escherichia coli (BL21) and assayed in right side out membrane vesicles. ScdF catalyzed the sodium-coupled transport of succinate and α-ketoglutarate. Succinate transport was strongly inhibited by malate, fumarate, tartrate, oxaloacetate and L-aspartate. Similar to the other DASS transporters, succinate transport by SdcF was inhibited by anthranilic acids, N-(p-amylcinnamoyl) anthranilic acid and flufenamate. SdcF transport was cation-dependent, with a K₀.₅ for sodium of ~1.5 mM and a K₀.₅ for Li⁺ of ~40 mM. Succinate transport kinetics by SdcF were sigmoidal, suggesting that SdcF may contain two cooperative substrate binding sites. The results support an ordered binding mechanism for SdcF in which sodium binds first and succinate binds last. We conclude that SdcF is a secondary active transporter for four- and five-carbon dicarboxylates that can use Na⁺ or Li⁺ as a driving cation.
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