SATP (YaaH), a succinate-acetate transporter protein in Escherichia coli

Joana Sá-Pessoa, Sandra Paiva, David Ribas, Inês Jesus Silva, Sandra Cristina Viegas, Cecília Maria Arraiano, Margarida Casal*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

45 Citations (Scopus)

Abstract

In the present paper we describe a new carboxylic acid transporter in Escherichia coli encoded by the gene yaaH. In contrast to what had been described for other YaaH family members, the E. coli transporter is highly specific for acetic acid (a monocarboxylate) and for succinic acid (a dicarboxylate), with affinity constants at pH 6.0 of 1.24±0.13 mM for acetic acid and 1.18±0.10 mM for succinic acid. In glucose-grown cells the ΔyaaH mutant is compromised for the uptake of both labelled acetic and succinic acids. YaaH, together with ActP, described previously as an acetate transporter, affect the use of acetic acid as sole carbon and energy source. Both genes have to be deleted simultaneously to abolish acetate transport. The uptake of acetate and succinate was restored when yaaH was expressed in trans in ΔyaaH ΔactP cells. We also demonstrate the critical role of YaaH amino acid residues Leu131 and Ala164 on the enhanced ability to transport lactate. Owing to its functional role in acetate and succinate uptake we propose its assignment as SatP: the Succinate-Acetate Transporter Protein.

Original languageEnglish
Pages (from-to)585-589
Number of pages5
JournalBiochemical Journal
Volume454
Issue number3
DOIs
Publication statusPublished - 15 Sep 2013
Externally publishedYes

Keywords

  • Acetate
  • Bacteria
  • Succinate
  • YaaH transport family
  • Yeast

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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