hiv- 1 protease inhibits cap- and poly(a)-dependent translation upon eif4gi and pabp cleavagehiv - 1蛋白酶抑制帽,保利(a)端依赖翻译eif4gi和与解理.pdfVIP

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hiv- 1 protease inhibits cap- and poly(a)-dependent translation upon eif4gi and pabp cleavagehiv - 1蛋白酶抑制帽,保利(a)端依赖翻译eif4gi和与解理.pdf

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hiv- 1 protease inhibits cap- and poly(a)-dependent translation upon eif4gi and pabp cleavagehiv - 1蛋白酶抑制帽,保利(a)端依赖翻译eif4gi和与解理

HIV- 1 Protease Inhibits Cap- and Poly(A)-Dependent Translation upon eIF4GI and PABP Cleavage ´ 1¤a 2¤b ´ 1 1 ´ 1 Alfredo Castello , David Franco , Pablo Moral-Lopez , Juan J. Berlanga , Enrique Alvarez , Eckard 2 1 Wimmer , Luis Carrasco * ´ ´ ´ 1 Centro de Biologıa Molecular ‘‘Severo Ochoa’’ (CSIC-UAM), Nicolas Cabrera 1, Universidad Autonoma de Madrid, Cantoblanco, Spain, 2 State University of New York at Stony Brook, Long Island, New York, United States of America Abstract A number of viral proteases are able to cleave translation initiation factors leading to the inhibition of cellular translation. This is the case of human immunodeficiency virus type 1 protease (HIV-1 PR), which hydrolyzes eIF4GI and poly(A)-binding protein (PABP). Here, the effect of HIV-1 PR on cellular and viral protein synthesis has been examined using cell-free systems. HIV-1 PR strongly hampers translation of pre-existing capped luc mRNAs, particularly when these mRNAs contain a poly(A) tail. In fact, HIV-1 PR efficiently blocks cap- and poly(A)-dependent translation initiation in HeLa extracts. Addition of exogenous PABP to HIV-1 PR treated extracts partially restores the translation of polyadenylated luc mRNAs, suggesting that PABP cleavage is directly involved in the inhibition of poly(A)-dependent translation. In contrast to these data, PABP cleavage induced by HIV-1 PR has little impact on the translation of polyadenylated encephalomyocarditis virus internal ribosome entry site (IRES)-containing mRNAs. In this case, the loss of poly(A)-dependent translation is compensated by t