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Selenium metabolism in prokaryotes

  • Chapter
Selenium

Summary

The biosynthesis and specific incorporation of selenocysteine into protein requires the function of a UGA codon determining the position of selenocysteine insertion and a secondary/tertiary structure within the mRNA, designated the SECIS element, following the UGA at its 3′side in bacteria and located in the 3′non-translated region in archaea. Biosynthesis of selenocysteine takes place on a unique tRNA species, tRNASec, which is charged by seryl-tRNA synthetase and serves as an adaptor for the conversion of the seryl moiety into the selenocysteyl product by selenocysteine synthase. Monoselenophosphate, provided by selenophosphate synthetase, is the selenium donor. Selenocysteyl-tRNASec is bound by the special translation factor SelB, which in bacteria via its C-terminal extension interacts with the apical part of the SECIS stem-loop structure. Crystallographic and NMR structural analyses of this extension from Moorella thermoacetica SelB, either free or complexed with the SECIS element, showed that it is made up of four winged helix domains from which only the C-terminal one interacts with the RNA ligand. Structure of the entire SelB molecule from Methanococcus maripaludis in the apo- and GDP/GTP bound forms revealed that it is a chimera between elongation factor Tu and initiation factors. Comparison of the structures in the GDP and GTP forms and modelling of the interactions between selenocysteyl-tRNA and SelB provided information on how SelB may discriminate tRNASec from canonical tRNAs and may differentiate between the selenocysteyl moiety and the seryl-residue of the precursor. A scenario for the major steps in the decoding process is postulated and arguments are given why the interaction of SelB with the mRNA is crucial. Reasons are also presented for the necessity of a balanced ratio of the components of the selenocysteine insertion apparatus and how it is regulated in E. coli via translational repression implicating a SECIS-like element located at the ultimate 5′end of selAB mRNA.

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Author information

Authors and Affiliations

  1. Lehrstuhl für Mikrobiologie der Universität München, D-80638, Munich, Germany

    August Böck & Michael Rother

  2. Institute of Molecular Biology and Biophysics, Swiss Federal Institute of Technology, ETH Hönggerberg, HPK building, CH-8093, Zürich, Switzerland

    Marc Leibundgut & Nenad Ban

Authors
  1. August Böck
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  2. Michael Rother
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  3. Marc Leibundgut
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  4. Nenad Ban
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Editor information

Editors and Affiliations

  1. National Cancer Institute, USA

    Dolph L. Hatfield

  2. University of Hawaii, USA

    Marla J. Berry

  3. Univeristy of Nebraska, USA

    Vadim N. Gladyshev

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© 2006 Springer Science+Business Media, LLC

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Böck, A., Rother, M., Leibundgut, M., Ban, N. (2006). Selenium metabolism in prokaryotes. In: Hatfield, D.L., Berry, M.J., Gladyshev, V.N. (eds) Selenium. Springer, Boston, MA. https://doi.org/10.1007/0-387-33827-6_2

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