Key result
The HIV-1 internal ribosome entry site relies on ribosomal protein S25 to recruit the 40S subunit directly to the initiation site without ribosome scanning.
The HIV-1 IRES recruits the 40S ribosomal subunit directly at the initiation site without scanning, relying on ribosomal protein S25.
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Suggests eS25 as a candidate for HIV-1 translation inhibition; leaves open clinical translation from this animal model.
The 5' leader of the HIV-1 genomic RNA is a multifunctional region that folds into secondary/tertiary structures that regulate multiple processes during viral replication including translation initiation. In this work, we examine the internal ribosome entry site (IRES) located in the 5' leader that drives translation initiation of the viral Gag protein under conditions that hinder cap-dependent translation initiation. We show that activity of the HIV-1 IRES relies on ribosomal protein S25 (eS25). Additionally, a mechanistic and mutational analysis revealed that the HIV-1 IRES is modular in nature and that once the 40S ribosomal subunit is recruited to the IRES, translation initiates without the need of ribosome scanning. These findings elucidate a mechanism of initiation by the HIV-1 IRES whereby a number of highly structured sites present within the HIV-1 5' leader leads to the recruitment of the 40S subunit directly at the site of initiation of protein synthesis.
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Carvajal et al. (2016) studied HIV-1. HIV-1 IRES and ribosomal protein S25 was evaluated on Translation initiation mechanism. The HIV-1 internal ribosome entry site relies on ribosomal protein S25 to recruit the 40S subunit directly to the initiation site without ribosome scanning.
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