Topic
Thiosulfate binding
About: Thiosulfate binding is a research topic. Over the lifetime, 11 publications have been published within this topic receiving 444 citations.
Papers
TL;DR: The sequence of 1,973 nucleotides encompassing the region at and directly adjacent to the CysB-dependent promoter controlling expression and synthesis of the sulfate-thiosulfate transport system of Escherichia coli has been determined and the deduced amino acid sequence of the cysP polypeptide indicates the presence of a signal peptide.
Abstract: The sequence of 1,973 nucleotides encompassing the region at and directly adjacent to the CysB-dependent promoter controlling expression and synthesis of the sulfate-thiosulfate transport system of Escherichia coli has been determined. The transcription start site has been mapped by primer extension. One open reading frame representing the first gene of the presumed sulfate transport operon was identified and designated cysP. The deduced amino acid sequence of the CysP polypeptide indicates the presence of a signal peptide. Expression of the cysP gene in the T7 promoter-polymerase system revealed the location of the gene product in the periplasm. Construction of a cysP insertional mutant and assays of binding and uptake of sulfate and thiosulfate by this mutant allowed the identification of the cysP gene product as a thiosulfate-binding protein. The TGA termination codon of cysP was found to overlap the putative ATG initiation codon of the next open reading frame, inferred as being essential for the sulfate transport system, and it was designated cysT. Preliminary sequence data from the corresponding region of the Salmonella typhimurium chromosome showed strictly homologous counterparts of the E. coli cysP and cysT genes.
110 citations
TL;DR: In Escherichia coli, the single cysP and sbp mutants are able to utilize both sulfate and thiosulfate as a sole sulfur source, while the inactivation of both genes leads to cysteine auxotrophy resulting from the block in the transport of both ions.
Abstract: In Escherichia coli, sulfate and thiosulfate ions are transported by an ABC-type transporter consisting of both the membrane components (the products of cysT, cysW, and cysA genes) and the periplasmic binders (the products of cysP and sbp genes). The single cysP and sbp mutants are able to utilize both sulfate and thiosulfate as a sole sulfur source, while the inactivation of both genes leads to cysteine auxotrophy resulting from the block in the transport of both ions.
100 citations
TL;DR: The kinetic behavior of rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.1) was investigated at pH values from 5.0 to 10.8 and a formal mechanism, combined with previous results, suggests a chemical interpretation on the following basis.
68 citations
TL;DR: It is inferred from findings that a cationic binding group for thiosulfate is present at the active site, and it is found to involve charge neutralization as evidenced by solvent and salt effects on the Michaelis constant.
55 citations
TL;DR: The biochemical characterization of E. coli SseA allowed the identification of the first prokaryotic protein with a preference for 3‐mercaptopyruvate as donor substrate, and substitution of Ser240 with an ionizable residue (Lys) increased the affinity for thiosulfate.
34 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2015 | 1 |
| 2006 | 1 |
| 2004 | 2 |
| 2001 | 1 |
| 2000 | 1 |
| 1995 | 1 |