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Selenium Metabolism in Prokaryotes

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Selenium

Abstract

Biologically active selenium occurs as a modification in tRNA, noncovalently attached cofactor, or as the amino acid selenocysteine, exerting functions key to the metabolism of the organism harboring it. In prokaryotes, selenocysteine is found in the catalytic site of numerous redox-active enzymes. It was designated as the 21st genetically encoded amino acid because it is cotranslationally inserted into growing polypeptides and universally encoded by the stop-codon UGA on the mRNA. The pathway of selenocysteine biosynthesis and incorporation is well understood in Bacteria, but considerable gaps of knowledge still exist in the respective system of the Archaea. This chapter aims to summarize details on prokaryal selenium biology with a focus on emphasizing the differences of the bacterial and the archaeal pathways of selenoprotein synthesis.

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Acknowledgements

I am deeply grateful to August Böck for having been my teacher and mentor; it was a privilege to be his graduate student. Work on the archaeal selenoprotein synthesis machinery in my laboratory is supported by grants from the Deutsche Forschungsgemeinschaft (via SFB 579).

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Authors and Affiliations

  1. Institut für Molekulare Biowissenschaften, Johann Wolfgang Goethe-Universität, Max-von-Laue-Str. 9, 60438, Frankfurt am Main, Germany

    Michael Rother

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  1. Michael Rother
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Correspondence to Michael Rother .

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Editors and Affiliations

  1. National Cancer Institute, Basic Research Laboratory, National Institutes of Health, Bethesda, 20892, Maryland, USA

    Dolph L. Hatfield

  2. University of Hawaii, Monoa, Dole Street 2444, Honolulu, 96822, Hawaii, USA

    Marla J. Berry

  3. , Division of Genetics, Department of Medi, Brigham and Women’s Hospital and Harvard, Avenue Louis Pasteur 77, Boston, 02115, USA

    Vadim N. Gladyshev

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Rother, M. (2011). Selenium Metabolism in Prokaryotes. In: Hatfield, D., Berry, M., Gladyshev, V. (eds) Selenium. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1025-6_36

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