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Gene Review

fdhF  -  formate dehydrogenase H

Escherichia coli CFT073

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Disease relevance of fdhF


High impact information on fdhF


Chemical compound and disease context of fdhF


Biological context of fdhF

  • Using a fluorescently labeled 17-nucleotide RNA minihelix that represents a binding site for the protein and that is part of the fdhF selenocysteine insertion sequence element positioned immediately downstream of the UGA triplet coding for selenocysteine incorporation, the kinetics of the interaction were studied [12].
  • We examined the positional effect of the UGA codon relative to the secondary structure on its decoding using a fdhF-lacZ fusion gene [13].
  • FHLA appears to bind to the upstream regulatory sequence (URS) in the 5' flanking region of the fdhF gene since activation of fdhF expression was dependent on the presence of the URS [14].
  • Escherichia coli possesses three distinct formate dehydrogenase enzymes encoded by the fdnGHI, fdhF, and fdoGHI operons [15].
  • A comparison of the nucleotide sequences and secondary mRNA structures corresponding to the selenoprotein A gene and the fdhF gene of Escherichia coli formate dehydrogenase shows that there is a similar potential for regulation of the specific insertion of selenocysteine at the UGA codon [16].

Anatomical context of fdhF


Associations of fdhF with chemical compounds

  • Lying at an approximately equal distance between both promoters was a short stretch of DNA which showed similarity to the sequence previously identified (Birkmann and Böck, 1989a) as being necessary for formate induction of the fdhF gene [18].
  • We designed seven different mRNA constructs derived from the fdhF mRNA which contain a translation initiation region including an AUG initiation codon followed by no, one, two, three, four, five or six UUC phenylalanine codon(s) and the UGA selenocysteine codon 5' adjacent to the fdhF mRNA hairpin [17].
  • Mutations blocking the synthesis of a functional molybdenum cofactor also had no major affect on fdhF and hyd expression [19].

Other interactions of fdhF

  • Efficient read-through of the UGA codon, as measured by beta-galactosidase activity and incorporation of selenium, was dependent on the presence of at least 40 bases of fdhF mRNA downstream of the UGA codon [20].

Analytical, diagnostic and therapeutic context of fdhF


  1. Coding from a distance: dissection of the mRNA determinants required for the incorporation of selenocysteine into protein. Heider, J., Baron, C., Böck, A. EMBO J. (1992) [Pubmed]
  2. Interspecies compatibility of selenoprotein biosynthesis in Enterobacteriaceae. Heider, J., Forchhammer, K., Sawers, G., Böck, A. Arch. Microbiol. (1991) [Pubmed]
  3. Genetic evidence that genes fdhD and fdhE do not control synthesis of formate dehydrogenase-N in Escherichia coli K-12. Stewart, V., Lin, J.T., Berg, B.L. J. Bacteriol. (1991) [Pubmed]
  4. Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Boyington, J.C., Gladyshev, V.N., Khangulov, S.V., Stadtman, T.C., Sun, P.D. Science (1997) [Pubmed]
  5. Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation. Tamura, T., Yamamoto, S., Takahata, M., Sakaguchi, H., Tanaka, H., Stadtman, T.C., Inagaki, K. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  6. Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli. Gladyshev, V.N., Khangulov, S.V., Axley, M.J., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  7. Targeted insertion of selenocysteine into the alpha subunit of formate dehydrogenase from Methanobacterium formicicum. Heider, J., Böck, A. J. Bacteriol. (1992) [Pubmed]
  8. 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]
  9. Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis. Gladyshev, V.N., Boyington, J.C., Khangulov, S.V., Grahame, D.A., Stadtman, T.C., Sun, P.D. J. Biol. Chem. (1996) [Pubmed]
  10. Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer. Khangulov, S.V., Gladyshev, V.N., Dismukes, G.C., Stadtman, T.C. Biochemistry (1998) [Pubmed]
  11. Escherichia coli genes whose products are involved in selenium metabolism. Leinfelder, W., Forchhammer, K., Zinoni, F., Sawers, G., Mandrand-Berthelot, M.A., Böck, A. J. Bacteriol. (1988) [Pubmed]
  12. Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA. Thanbichler, M., Bock, A., Goody, R.S. J. Biol. Chem. (2000) [Pubmed]
  13. Effect of the relative position of the UGA codon to the unique secondary structure in the fdhF mRNA on its decoding by selenocysteinyl tRNA in Escherichia coli. Chen, G.F., Fang, L., Inouye, M. J. Biol. Chem. (1993) [Pubmed]
  14. Identification and sequence analysis of the gene encoding the transcriptional activator of the formate hydrogenlyase system of Escherichia coli. Schlensog, V., Böck, A. Mol. Microbiol. (1990) [Pubmed]
  15. Coordinate regulation of the Escherichia coli formate dehydrogenase fdnGHI and fdhF genes in response to nitrate, nitrite, and formate: roles for NarL and NarP. Wang, H., Gunsalus, R.P. J. Bacteriol. (2003) [Pubmed]
  16. Selenoprotein A component of the glycine reductase complex from Clostridium purinolyticum: nucleotide sequence of the gene shows that selenocysteine is encoded by UGA. Garcia, G.E., Stadtman, T.C. J. Bacteriol. (1991) [Pubmed]
  17. Interaction of the Escherichia coli fdhF mRNA hairpin promoting selenocysteine incorporation with the ribosome. Hüttenhofer, A., Heider, J., Böck, A. Nucleic Acids Res. (1996) [Pubmed]
  18. Characterization of divergent NtrA-dependent promoters in the anaerobically expressed gene cluster coding for hydrogenase 3 components of Escherichia coli. Lutz, S., Böhm, R., Beier, A., Böck, A. Mol. Microbiol. (1990) [Pubmed]
  19. Factors affecting transcriptional regulation of the formate-hydrogen-lyase pathway of Escherichia coli. Birkmann, A., Zinoni, F., Sawers, G., Böck, A. Arch. Microbiol. (1987) [Pubmed]
  20. Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine. Zinoni, F., Heider, J., Böck, A. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  21. Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Leinfelder, W., Zehelein, E., Mandrand-Berthelot, M.A., Böck, A. Nature (1988) [Pubmed]
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