Translational repression by a novel partner of human poly(A) binding protein, Paip2

被引:178
|
作者
Khaleghpour, K
Svitkin, YV
Craig, AW
DeMaria, CT
Deo, RC
Burley, SK
Sonenberg, N [1 ]
机构
[1] McGill Univ, McGill Canc Ctr, Dept Biochem, Montreal, PQ H3G 1Y6, Canada
[2] Rockefeller Univ, Howard Hughes Med Inst, Labs Mol Biophys, New York, NY 10021 USA
关键词
D O I
10.1016/S1097-2765(01)00168-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The eukaryotic mRNA 3' poly(A) tail acts synergistically with the 5' cap structure to enhance translation. This effect is mediated by a bridging complex, composed of the poly(A) binding protein (PABP), eIF4G, and the cap binding protein, eIF4E. PABP-interacting protein 1 (Paip1) is another factor that interacts with PABP to coactivate translation. Here, we describe a novel human PABP-interacting protein (Paip2), which acts as a repressor of translation both in vitro and in vivo. Paip2 preferentially inhibits translation of a poly(A)-containing mRNA, but has no effect on the translation of hepatitis C virus mRNA, which is cap- and eIf4G-independent. Paip2 decreases the affinity of PABP for polyadenylate RNA, and disrupts the repeating structure of poly(A) ribonucleoprotein. Furthermore, Paip2 competes with Paip1 for PABP binding. Thus, Paip2 inhibits translation by interdicting PABP function.
引用
收藏
页码:205 / 216
页数:12
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