Publications
2017
Haimov O, Sinvani H, Martin F, Ulitsky I, Emmanuel R, Tamarkin-Ben-Harush A, Vardy A, Dikstein R
Efficient and Accurate Translation Initiation Directed by TISU Involves RPS3 and RPS10e Binding and Differential Eukaryotic Initiation Factor 1A Regulation Article de journal
Dans: Mol Cell Biol, vol. 37, no. 15, p. e00150-00117, 2017, ISBN: 28584194.
Résumé | Liens | BibTeX | Étiquettes: ERIANI, RPS10 RPS10e RPS3 TISU eIF1A short 5′UTR translation initiation, Unité ARN
@article{,
title = {Efficient and Accurate Translation Initiation Directed by TISU Involves RPS3 and RPS10e Binding and Differential Eukaryotic Initiation Factor 1A Regulation},
author = {O Haimov and H Sinvani and F Martin and I Ulitsky and R Emmanuel and A Tamarkin-Ben-Harush and A Vardy and R Dikstein},
url = {https://www.ncbi.nlm.nih.gov/pubmed/28584194?dopt=Abstract},
doi = {10.1128/MCB.00150-17},
isbn = {28584194},
year = {2017},
date = {2017-01-01},
journal = {Mol Cell Biol},
volume = {37},
number = {15},
pages = {e00150-00117},
abstract = {Canonical translation initiation involves ribosomal scanning but short 5' UTR mRNAs are translated in a scanning-independent manner. The extent and mechanism of scanning independent translation is not fully understood. Here we report that short 5' UTR mRNAs constitute a substantial fraction of the translatome. Short 5' UTR mRNAs are enriched with TISU, a 12-nucleotide element directing efficient scanning-independent translation. Comprehensive mutagenesis revealed that each AUG flanking nucleotides of TISU contributes to translational strength but only few are important for accuracy. Using site-specific UV crosslinking of ribosomal complexes assembled on TISU mRNA we demonstrate specific binding of TISU to ribosomal proteins at the E and the A sites. We identified RPS3 as the major TISU-binding protein in the 48S complex A-site. Upon 80S formation RPS3 interaction is weakened and switched to RPS10e (former name RPS10). We further demonstrate that TISU is particularly dependent on eIF1A which interacts with both RPS3 and RPS10e. Our findings suggest that the cap-recruited ribosome specifically binds the TISU nucleotides at the A and the E sites in cooperation with eIF1A to promote scanning arrest.},
keywords = {ERIANI, RPS10 RPS10e RPS3 TISU eIF1A short 5′UTR translation initiation, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Canonical translation initiation involves ribosomal scanning but short 5' UTR mRNAs are translated in a scanning-independent manner. The extent and mechanism of scanning independent translation is not fully understood. Here we report that short 5' UTR mRNAs constitute a substantial fraction of the translatome. Short 5' UTR mRNAs are enriched with TISU, a 12-nucleotide element directing efficient scanning-independent translation. Comprehensive mutagenesis revealed that each AUG flanking nucleotides of TISU contributes to translational strength but only few are important for accuracy. Using site-specific UV crosslinking of ribosomal complexes assembled on TISU mRNA we demonstrate specific binding of TISU to ribosomal proteins at the E and the A sites. We identified RPS3 as the major TISU-binding protein in the 48S complex A-site. Upon 80S formation RPS3 interaction is weakened and switched to RPS10e (former name RPS10). We further demonstrate that TISU is particularly dependent on eIF1A which interacts with both RPS3 and RPS10e. Our findings suggest that the cap-recruited ribosome specifically binds the TISU nucleotides at the A and the E sites in cooperation with eIF1A to promote scanning arrest.