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Easing selenocysteine into proteins

Nature Structural & Molecular Biology volume 14, pages 100–101 (2007)Cite this article

Selenocysteinyl-tRNASec is used by many organisms from all three domains of life to incorporate selenocysteine (Sec) site-specifically into certain proteins. Two recent reports have identified a new Sec synthase that catalyzes the last step in the generation of this aminoacyl-tRNA in eukarya and archaea.

The ability of SerRS to misacylate tRNASec is universally conserved in selenium-using organisms and has been documented in representative archaea9 and eukarya10. However, as only a few archaea and no eukarya carry a SelA-like protein, it was unclear how Ser-tRNASec is converted into Sec-tRNASec in these organisms. Furthermore, the archaeal SelA-like protein from Methanocaldococcus jannaschii (MJ0158) was shown to be inactive as a Sec synthase11.

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Figure 1: Selenocysteine can be incorporated into specific proteins via read-through of an internal, in-frame UGA codon.
Figure 2: The biosynthesis of Sec-tRNASec in bacteria (top pathway) and in archaea and eukarya (bottom pathway).

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  1. Tamara L. Hendrickson is in the Department of Chemistry, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland 21218, USA. tamara.hendrickson@jhu.edu,

    Tamara L Hendrickson

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Hendrickson, T. Easing selenocysteine into proteins. Nat Struct Mol Biol 14, 100–101 (2007). https://doi.org/10.1038/nsmb0207-100

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