Abstract
Selenoproteins with known functions are oxidoreductase enzymes that serve roles in maintaining cellular redox balance, reproductive health, thyroid hormone metabolism, development, and immune functions. Unique to selenoprotein biosynthesis is the requirement during translation to redefine an in-frame UGA codon to encode for selenocysteine rather than terminate translation. This non-canonical translation event is a bottleneck in selenoprotein synthesis and subject to gene-specific regulation. Here, the application of ribosome profiling, which involves deep sequencing of ribosome protected mRNA fragments, to examine mechanisms of selenoprotein biosynthesis will be discussed. The ability of this technique to quantify ribosome abundance and position, at codon resolution, on selenoprotein mRNAs has provided important insight into long-standing questions regarding the efficiency and regulation of selenocysteine incorporation as well as provoking new questions for future investigations.
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Acknowledgments
I would like to acknowledge Dr. Dolph Hatfield and Bradley Carlson (NIH) for their insight and experimental contributions towards the development of ribosome profiling for analysis of selenoprotein expression; Brian Dalley, Lisa Baird, and Christine Anderson (University of Utah) for their technical expertise; and Drs. Raymond Gesteland and John Atkins (University of Utah) for their many years of encouragement and advice. This work was supported by NIH grants GM114291 (M.T.H.) and ES0022716 (M.T.H.).
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Howard, M.T. (2016). Probing Selenoprotein Translation by Ribosome Profiling. In: Hatfield, D., Schweizer, U., Tsuji, P., Gladyshev, V. (eds) Selenium. Springer, Cham. https://doi.org/10.1007/978-3-319-41283-2_3
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DOI: https://doi.org/10.1007/978-3-319-41283-2_3
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