Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (250K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (26)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Hohsaka, T.
Right arrow Articles by Sisido, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hohsaka, T.
Right arrow Articles by Sisido, M.
Related Collections
Right arrow Mutagenesis
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2001, Vol. 29, No. 17 3646-3651
© 2001 Oxford University Press

Five-base codons for incorporation of nonnatural amino acids into proteins

Takahiro Hohsaka, Yuki Ashizuka, Hiroshi Murakami and Masahiko Sisido*

Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, 3-1-1 Tsushimanaka, Okayama 700-8530, Japan

Extension of the genetic code for the introduction of nonnatural amino acids into proteins was examined by using five-base codon–anticodon pairs. A streptavidin mRNA containing a CGGUA codon at the Tyr54 position and a tRNAUACCG chemically aminoacylated with a nonnatural amino acid were added to an Escherichia coli in vitro translation system. Western blot analysis indicated that the CGGUA codon is decoded by the aminoacyl-tRNA containing the UACCG anticodon. HPLC analysis of the tryptic fragment of the translation product revealed that the nonnatural amino acid was incorporated corresponding to the CGGUA codon without affecting the reading frame adjacent to the CGGUA codon. Another 15 five-base codons CGGN1N2, where N1 and N2 indicate one of four nucleotides, were also successfully decoded by aminoacyl-tRNAs containing the complementary five-base anticodons. These results provide a novel strategy for nonnatural mutagenesis as well as a novel insight into the mechanism of frameshift suppression.

* To whom correspondence should be addressed. Tel: +81 86 251 8218; Fax: +81 86 251 8219; Email: sisido{at}cc.okayama-u.ac.jp


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Microbiol. Mol. Biol. Rev.Home page
J. F. Atkins and G. R. Bjork
A Gripping Tale of Ribosomal Frameshifting: Extragenic Suppressors of Frameshift Mutations Spotlight P-Site Realignment
Microbiol. Mol. Biol. Rev., March 1, 2009; 73(1): 178 - 210.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. C. Anderson, N. Wu, S. W. Santoro, V. Lakshman, D. S. King, and P. G. Schultz
An expanded genetic code with a functional quadruplet codon
PNAS, May 18, 2004; 101(20): 7566 - 7571.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. O'Connor
Insertions in the anticodon loop of tRNA1Gln(sufG) and tRNALys promote quadruplet decoding of CAAA
Nucleic Acids Res., May 1, 2002; 30(9): 1985 - 1990.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.