A cellular protein that binds to the 5'-noncoding region of poliovirus RNA: implications for internal translation initiation.
Key result
A 52-kD polypeptide (p52) from HeLa cell extracts was identified as part of a specific protein-RNA complex that forms with the 5'-noncoding region of poliovirus RNA.
Population
HeLa cell extract, reticulocyte lysate, wheat-germ extract, and poliovirus RNA fragment
Design
Preclinical
Authors
Discussion
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Member takes
Implication
Highlights potential host factors for viral IRES; leaves open their identity and mechanistic roles.
Structured PICO
P
Population
HeLa cell extract, reticulocyte lysate, wheat-germ extract, and poliovirus RNA fragment (nucleotides 559-624 of 5' UTR)
I
Intervention
Mobility-shift electrophoresis assay and UV cross-linking assay
O
Outcome
Identification of specific RNA-protein complex and associated polypeptidessurrogate
Identified a 52-kD cellular protein that binds to the poliovirus 5' UTR, which may be involved in internal translation initiation.
Cite This Study
Meerovitch et al. (1989) studied Poliovirus translation initiation. RNA fragment containing nucleotides 559-624 of the poliovirus 5' UTR vs. Reticulocyte lysate or wheat-germ extract was evaluated on RNA-protein complex formation. A 52-kD polypeptide (p52) from HeLa cell extracts was identified as part of a specific protein-RNA complex that forms with the 5'-noncoding region of poliovirus RNA.