skip to main content
DOE PAGES title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Facile Recoding of Selenocysteine in Nature

Abstract

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.

Authors:
 [1];  [1];  [2];  [1];  [2];  [2];  [2];  [3]
  1. Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry
  2. USDOE Joint Genome Institute (JGI), Walnut Creek, CA (United States)
  3. Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry, and Dept. of Chemistry
Publication Date:
Research Org.:
Yale Univ., New Haven, CT (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Chemical Sciences, Geosciences & Biosciences Division
OSTI Identifier:
1467447
Grant/Contract Number:  
FG02-98ER20311; AC02-05CH11231
Resource Type:
Accepted Manuscript
Journal Name:
Angewandte Chemie (International Edition)
Additional Journal Information:
Journal Name: Angewandte Chemie (International Edition); Journal Volume: 55; Journal Issue: 17; Journal ID: ISSN 1433-7851
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; genetic code; selenocysteine; sense codon recoding; metagenome; synthetic biology

Citation Formats

Mukai, Takahito, Englert, Markus, Tripp, H. James, Miller, Corwin, Ivanova, Natalia N., Rubin, Edward M., Kyrpides, Nikos C., and Söll, Dieter. Facile Recoding of Selenocysteine in Nature. United States: N. p., 2016. Web. doi:10.1002/anie.201511657.
Mukai, Takahito, Englert, Markus, Tripp, H. James, Miller, Corwin, Ivanova, Natalia N., Rubin, Edward M., Kyrpides, Nikos C., & Söll, Dieter. Facile Recoding of Selenocysteine in Nature. United States. doi:10.1002/anie.201511657.
Mukai, Takahito, Englert, Markus, Tripp, H. James, Miller, Corwin, Ivanova, Natalia N., Rubin, Edward M., Kyrpides, Nikos C., and Söll, Dieter. Wed . "Facile Recoding of Selenocysteine in Nature". United States. doi:10.1002/anie.201511657. https://www.osti.gov/servlets/purl/1467447.
@article{osti_1467447,
title = {Facile Recoding of Selenocysteine in Nature},
author = {Mukai, Takahito and Englert, Markus and Tripp, H. James and Miller, Corwin and Ivanova, Natalia N. and Rubin, Edward M. and Kyrpides, Nikos C. and Söll, Dieter},
abstractNote = {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.},
doi = {10.1002/anie.201511657},
journal = {Angewandte Chemie (International Edition)},
number = 17,
volume = 55,
place = {United States},
year = {2016},
month = {3}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Citation Metrics:
Cited by: 24 works
Citation information provided by
Web of Science

Save / Share:

Works referenced in this record:

Genetic Code Supports Targeted Insertion of Two Amino Acids by One Codon
journal, January 2009

  • Turanov, A. A.; Lobanov, A. V.; Fomenko, D. E.
  • Science, Vol. 323, Issue 5911, p. 259-261
  • DOI: 10.1126/science.1164748

Stop codon reassignments in the wild
journal, May 2014

  • Ivanova, N. N.; Schwientek, P.; Tripp, H. J.
  • Science, Vol. 344, Issue 6186, p. 909-913
  • DOI: 10.1126/science.1250691

Efficient Reassignment of a Frequent Serine Codon in Wild-Type Escherichia coli
journal, November 2015

  • Ho, Joanne M.; Reynolds, Noah M.; Rivera, Keith
  • ACS Synthetic Biology, Vol. 5, Issue 2, p. 163-171
  • DOI: 10.1021/acssynbio.5b00197