LARP1 specifically recognizes the 3' terminus of poly(A) mRNA.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Aoki K,Adachi S,Homoto M,Kusano H,Koike K,Natsume T

doi

10.1016/j.febslet.2013.05.035

subject

Has Abstract

pub_date

2013-07-11 00:00:00

pages

2173-8

issue

14

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(13)00389-X

journal_volume

587

pub_type

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