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Gene Review

selA  -  selenocysteine synthase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3580, JW3564, fdhA
 
 
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Disease relevance of selA

 

High impact information on selA

 

Chemical compound and disease context of selA

 

Biological context of selA

  • In contrast, the other three sel genes (selA, -B, and -D) were shown to be constituents of two unlinked operons [9].
  • By using Northern (RNA) gel blot analysis, the transcription start site was located within a 1.6-kilobase BglII-NcoI fragment 4.3 kilobases upstream from the fdhA gene [10].
  • Se is an essential trace element and is found as a selenocysteine in the active site of Se-enzymes, such as glutathione peroxidase. tRNASec is first aminoacylated with serine by Ser RS and further is converted to selenocysteyl-tRNA by selenocysteine synthase [11].
 

Associations of selA with chemical compounds

  • Analysis of amino acid sequences indicated that selenocysteine synthase belongs to the alpha/gamma superfamily of pyridoxal-5'-phosphate-dependent enzymes [8].
  • These data together with the finding that selenophosphate synthetase is highly specific for selenide indicate that the phosphate moiety of selenophosphate provides selenocysteine synthase with the discrimination specificity against sulfur [8].
  • It was found to be dependent on the positive control exerted by the fdhA, B and C genes, possibly involved in selenium incorporation, and by an hydB gene affecting the formate hydrogenlyase pathway [12].
  • The apparent molecular mass of the native enzyme was determined by gel filtration to be about 100 kDa, which was confirmed by the fdhA nucleotide sequence. fdhA encodes for a pre-protein that differs from the truncated mature protein by an N-terminal 35-amino-acid signal peptide containing a twin arginine motif [13].
  • The soluble periplasmic subunit of the formate dehydrogenase FdhA of the tetrachloroethene-reducing anaerobe Sulfurospirillum multivorans was purified to apparent homogeneity and the gene ( fdhA) was identified and sequenced [13].
 

Other interactions of selA

  • Guided by principal component analysis, we instead discovered that the most efficient bacterial selenoprotein production conditions were obtained with the high-transcription T7lac-driven pET vector system in presence of the selA, selB, and selC genes, with induction of production at late exponential phase [14].

References

  1. Selenocysteine synthase from Escherichia coli. Nucleotide sequence of the gene (selA) and purification of the protein. Forchhammer, K., Leinfelder, W., Boesmiller, K., Veprek, B., Böck, A. J. Biol. Chem. (1991) [Pubmed]
  2. Selenophosphate as a substrate for mammalian selenocysteine synthase, its stability and toxicity. Mizutani, T., Kanaya, K., Tanabe, K. Biofactors (1999) [Pubmed]
  3. In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product. Leinfelder, W., Forchhammer, K., Veprek, B., Zehelein, E., Böck, A. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  4. The length of the aminoacyl-acceptor stem of the selenocysteine-specific tRNA(Sec) of Escherichia coli is the determinant for binding to elongation factors SELB or Tu. Baron, C., Böck, A. J. Biol. Chem. (1991) [Pubmed]
  5. Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence. Forchhammer, K., Böck, A. J. Biol. Chem. (1991) [Pubmed]
  6. Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis. Forchhammer, K., Rücknagel, K.P., Böck, A. J. Biol. Chem. (1990) [Pubmed]
  7. Structural and functional investigation of a putative archaeal selenocysteine synthase. Kaiser, J.T., Gromadski, K., Rother, M., Engelhardt, H., Rodnina, M.V., Wahl, M.C. Biochemistry (2005) [Pubmed]
  8. Bacterial selenocysteine synthase--structural and functional properties. Tormay, P., Wilting, R., Lottspeich, F., Mehta, P.K., Christen, P., Böck, A. Eur. J. Biochem. (1998) [Pubmed]
  9. Expression and operon structure of the sel genes of Escherichia coli and identification of a third selenium-containing formate dehydrogenase isoenzyme. Sawers, G., Heider, J., Zehelein, E., Böck, A. J. Bacteriol. (1991) [Pubmed]
  10. Characterization of the upstream region of the formate dehydrogenase operon of Methanobacterium formicicum. Patel, P.S., Ferry, J.G. J. Bacteriol. (1988) [Pubmed]
  11. The dual identities of mammalian tRNA(Sec) for SerRS and selenocysteine synthase. Mizutani, T., Kanaya, K., Ikeda, S., Fujiwara, T., Yamada, K., Totsuka, T. Mol. Biol. Rep. (1998) [Pubmed]
  12. Regulation of the fdhF gene encoding the selenopolypeptide for benzyl viologen-linked formate dehydrogenase in Escherichia coli. Wu, L.F., Mandrand-Berthelot, M.A. Mol. Gen. Genet. (1987) [Pubmed]
  13. Purification and properties of the formate dehydrogenase and characterization of the fdhA gene of Sulfurospirillum multivorans. Schmitz, R.P., Diekert, G. Arch. Microbiol. (2003) [Pubmed]
  14. Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis. Rengby, O., Johansson, L., Carlson, L.A., Serini, E., Vlamis-Gardikas, A., Kårsnäs, P., Arnér, E.S. Appl. Environ. Microbiol. (2004) [Pubmed]
 
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