Ribosomal frameshifting in decoding antizyme mRNAs from yeast and protists to humans: close to 300 cases reveal remarkable diversity despite underlying conservation

Loading...
Thumbnail Image
Files
3919.pdf(8.48 MB)
Published Version
3919-1.doc(31 KB)
Extracted File 1
3919-2.pdf(986.83 KB)
Extracted File 2
3919-3.pdf(1.04 MB)
Extracted File 3
3919-4.pdf(1.01 MB)
Extracted File 4
Date
2007
Authors
Ivanov, Ivaylo P.
Atkins, John F.
Journal Title
Journal ISSN
Volume Title
Publisher
Oxford University Press
Published Version
Research Projects
Organizational Units
Journal Issue
Abstract
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.
Description
Keywords
Ornithine-decarboxylase antizyme , Zebrafish danio-rerio , Escherichia-coli , Cell growth , Polyamine transport , Mammalian antizyme , Regulatory protein , Release factor-2 , Drosophila gene , Fission yeast
Citation
Ivanov, I. P. and Atkins, J. F. (2007) 'Ribosomal frameshifting in decoding antizyme mRNAs from yeast and protists to humans: close to 300 cases reveal remarkable diversity despite underlying conservation', Nucleic Acids Research, 35(6), pp. 1842-1858. doi: 10.1093/nar/gkm035