Facile Recoding of Selenocysteine in Nature

Mukai, Takahito; Englert, Markus; Tripp, H. James; Miller, Corwin; Ivanova, Natalia N.; Rubin, Edward M.; Kyrpides, Nikos C.; Söll, Dieter

doi:10.1002/anie.201511657

Facile Recoding of Selenocysteine in Nature

Journal Article · Wed Mar 16 04:00:00 EDT 2016 · Angewandte Chemie (International Edition)

DOI:https://doi.org/10.1002/anie.201511657· OSTI ID:1467447

Mukai, Takahito ^[1]; Englert, Markus ^[2]; Tripp, H. James ^[3]; Miller, Corwin ^[2]; Ivanova, Natalia N. ^[3]; Rubin, Edward M. ^[3]; Kyrpides, Nikos C. ^[3]; Söll, Dieter ^[4]

Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry; Yale Univ., New Haven, CT (United States)
Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry
USDOE Joint Genome Institute (JGI), Walnut Creek, CA (United States)
Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry, and Dept. of Chemistry

Selenocysteine (Sec or U) is encoded by UGA, a stop codon reassigned by a Sec-specific elongation factor and a distinctive RNA structure. To discover possible code variations in extant organisms we analyzed 6.4 trillion base pairs of metagenomic sequences and 24,903 microbial genomes for tRNASec species. As expected, UGA is the predominant Sec codon in use. We also found tRNASec species that recognize the stop codons UAG and UAA, and ten sense codons. Selenoprotein synthesis programmed by UAG in Geodermatophilus and Blastococcus, and by the Cys codon UGU in Aeromonas salmonicida was confirmed by metabolic labeling with 75Se or mass spectrometry. Other tRNASec species with different anticodons enabled Escherichia coli to synthesize active formate dehydrogenase H, a selenoenzyme. This illustrates the ease by which the genetic code may evolve new coding schemes, possibly aiding organisms to adapt to changing environments. Lastly, our results reveal that the genetic code is much more flexible than previously thought.

View Accepted Manuscript (DOE)

Research Organization:: Yale Univ., New Haven, CT (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Chemical Sciences, Geosciences & Biosciences Division

Grant/Contract Number:: FG02-98ER20311; AC02-05CH11231

OSTI ID:: 1467447

Journal Information:: Angewandte Chemie (International Edition), Journal Name: Angewandte Chemie (International Edition) Journal Issue: 17 Vol. 55; ISSN 1433-7851

Publisher:: WileyCopyright Statement

Country of Publication:: United States

Language:: English

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