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LARP1 specifically recognizes the 3′ terminus of poly(A) mRNA
Author(s) -
Aoki Kazuma,
Adachi Shungo,
Homoto Masae,
Kusano Hideo,
Koike Katsuyuki,
Natsume Tohru
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.05.035
Subject(s) - messenger rna , chemistry , microbiology and biotechnology , biology , biochemistry , gene
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.