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Biochim Biophys Acta. 2009 Nov;1790(11):1404-14. doi: 10.1016/j.bbagen.2009.03.010. Epub 2009 Mar 27.

The many levels of control on bacterial selenoprotein synthesis.

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  • 1Laboratoire de Chimie et Biologie Structurales, FRC3115, ICSN-CNRS, 1 ave de la terrasse, 91190 Gif-sur-Yvette, France.


Selenium shares many chemical facets with sulphur but differs from it in the redox potential, especially of the Se(2-)/S(2-) oxidation state. The higher chemical reactivity of the deprotonated selenol has been used by Biology in the synthesis of the amino acid selenocysteine and its DNA-encoded incorporation into specific positions of proteins to enhance their structural role or their activity. Since selenocysteine is a steric isomer of cysteine, numerous control mechanisms have been developed which prevent cross-intrusion of the elements during biosynthesis and insertion. As described in this review, these fidelity steps occur at the genetic, biochemical and physiological level.

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