Nucleic Acids Research Advance Access originally published online on March 1, 2007
Nucleic Acids Research 2007 35(6):1842-1858; doi:10.1093/nar/gkm035
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Nucleic Acids Research, 2007, Vol. 35, No. 6 1842-1858
© 2007 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-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Ribosomal frameshifting in decoding antizyme mRNAs from yeast and protists to humans: close to 300 cases reveal remarkable diversity despite underlying conservation
1Biosciences Institute, University College Cork, Cork, Ireland and 2Department of Human Genetics, University of Utah, Salt Lake City, UT 84112-5330, USA
*Correspondence may be addressed to either author at Tel: +1-353 21 490 1313; Fax: +1-353 23 55147; Emails: iivanov{at}genetics.utah.edu and j.atkins{at}ucc.ie
Received November 16, 2006. Revised January 5, 2007. Accepted January 7, 2007.
The protein antizyme is a negative regulator of intracellular polyamine levels. Ribosomes synthesizing antizyme start in one ORF and at the codon 5' adjacent to its stop codon, shift +1 to a second and partially overlapping ORF which encodes most of the protein. The ribosomal frameshifting is a sensor and effector of an autoregulatory circuit which is conserved in animals, fungi and protists. Stimulatory signals encoded 5' and 3' of the shift site act to program the frameshifting. Despite overall conservation, many individual branches have evolved specific features surrounding the frameshift site. Among these are RNA pseudoknots, RNA stem-loops, conserved primary RNA sequences, nascent peptide sequences and branch-specific ‘shifty’ codons.
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