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Nucleic Acids Research Advance Access originally published online on August 18, 2006
Nucleic Acids Research 2006 34(15):4302-4310; doi:10.1093/nar/gkl531
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Nucleic Acids Research, 2006, Vol. 34, No. 15 4302-4310
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commerical use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Antisense-induced ribosomal frameshifting

Clark M. Henderson, Christine B. Anderson and Michael T. Howard*

Department of Human Genetics, University of Utah 15 N 2030 E, Room 7410, Salt Lake City, UT 84112-5330, USA

*To whom correspondence should be addressed. Tel: +1 801 585 1927; Fax: +1 801 585 3910; Email: mhoward{at}genetics.utah.edu

Received February 9, 2006. Revised June 7, 2006. Accepted July 7, 2006.

Programmed ribosomal frameshifting provides a mechanism to decode information located in two overlapping reading frames by diverting a proportion of translating ribosomes into a second open reading frame (ORF). The result is the production of two proteins: the product of standard translation from ORF1 and an ORF1–ORF2 fusion protein. Such programmed frameshifting is commonly utilized as a gene expression mechanism in viruses that infect eukaryotic cells and in a subset of cellular genes. RNA secondary structures, consisting of pseudoknots or stem–loops, located downstream of the shift site often act as cis-stimulators of frameshifting. Here, we demonstrate for the first time that antisense oligonucleotides can functionally mimic these RNA structures to induce +1 ribosomal frameshifting when annealed downstream of the frameshift site, UCC UGA. Antisense-induced shifting of the ribosome into the +1 reading frame is highly efficient in both rabbit reticulocyte lysate translation reactions and in cultured mammalian cells. The efficiency of antisense-induced frameshifting at this site is responsive to the sequence context 5' of the shift site and to polyamine levels.


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