Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 9, Pages 859-864Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3280
Keywords
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Funding
- NIH [GM047467, EB002026, R01 AI51340]
- Japan Society for the Promotion of Science (JSPS) Postdoctoral Fellowships for Research Abroad
- Daiichi-Sankyo Foundation of Life Science
- Naito Foundation
- Department of Energy (DOE) Integrated Diffraction Analysis (IDAT) grant [DE-AC02-05CH11231]
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Many viruses bypass canonical cap-dependent translation in host cells by using internal ribosomal entry sites (IRESs) in their transcripts; IRESs hijack initiation factors for the assembly of initiation complexes. However, it is currently unknown how 1RES RNAs recognize initiation factors that have no endogenous RNA binding partners; in a prominent example, the IRES of encephalomyocarditis virus (EMCV) interacts with the HEAT-1 domain of eukaryotic initiation factor 4G (eIF4G). Here we report the solution structure of the J-K region of this 1RES and show that its stems are precisely organized to position protein-recognition bulges. This multisite interaction mechanism operates on an all-or-nothing principle in which all domains are required. This preorganization is accomplished by an 'adjuster module': a pentaloop motif that acts as a dual-sided docking station for base pair receptors. Because subtle changes in the orientation abrogate protein capture, our study highlights how a viral RNA acquires affinity for a target protein.
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