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Science 2 December 2005:
Vol. 310. no. 5753, p. 1385
DOI: 10.1126/science.310.5753.1385m
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The mammalian translation factor eIF3 (a complex of about 750 kilodaltons) prevents premature association of the large and small ribosome subunits; it is involved in start codon detection; and it assists in the assembly of active ribosomes. In addition, eIF3 recruits messenger RNA (mRNA) bearing either a methylated guanosine cap at the 5′-end or an internal ribosome entry site (IRES) to the small subunit of the ribosome. Using cryoelectron microscopy reconstructions, single-particle analysis, and modeling, Siridechadilok et al. (p. 1513) now elucidate the structure and interactions of eIF3. eIF3 interacts with the hepatitis C virus (HCV) IRES RNA and the 5′-cap binding complex eIF4F via the same domain to position the mRNA strand near the exit site of the 40S ribosomal subunit. This work provides structural insight for translational regulation by eIF3, including the prevention of premature ribosome assembly.




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