LARP1 specifically recognizes the 3′ terminus of poly(A) mRNA
| Autor: | Tohru Natsume, Kazuma Aoki, Hideo Kusano, Shungo Adachi, Katsuyuki Koike, Masae Homoto |
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| Rok vydání: | 2013 |
| Předmět: |
Proteomics
RNA-directed immunoprecipitation Proteome Polyadenylation RNA Stability Molecular Sequence Data Biophysics Gene Expression LAPP1 Plasma protein binding Biology Autoantigens Poly(A)-Binding Protein I Biochemistry DNA-binding protein Poly(A) tail Structural Biology Gene expression Genetics Humans RNA Messenger RNA Small Interfering Molecular Biology Regulation of gene expression Messenger RNA Base Sequence RNA Translation (biology) Cell Biology Molecular biology Cell biology HEK293 Cells Gene Expression Regulation Ribonucleoproteins Gene Knockdown Techniques Poly A Protein Binding 5′TOP mRNA |
| Zdroj: | FEBS Letters. 587:2173-2178 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2013.05.035 |
| Popis: | A poly(A) tail functions in mRNA turnover and in facilitating translation as a ribonucleoprotein complex with poly(A) binding proteins (PABPs). However, factors that associate with the poly(A) tail other than PABPs have not been described. Using proteomics, we identified candidate proteins that interact to the 3′ terminus of the poly(A) tail. Among these proteins, we focused on La motif-related protein 1 (LARP1) and found that LARP1 specifically recognizes the 3′ termini of normal poly(A) tails. We also reveal that LARP1 stabilizes multiple mRNAs carrying 5′ terminal oligopyrimidine tract (5′TOP). Our findings suggest that LARP1 may be involved in the post-transcriptional regulation of gene expression, at least in several 5′TOP mRNAs, through the binding to 3′ terminus of the poly(A) tail. |
| Databáze: | OpenAIRE |
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