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Vol. 14, No. 4, pp. 414-421, February 15, 2000
Department of Microbiology, New York University School of Medicine,
New York, New York 10016 USA
Translation initiation on eukaryotic mRNAs involves 40S ribosome
association with mRNA caps (m7GpppN), mediated by initiation
factor eIF4F. 40S eukaryotic ribosomes and initiation factors undergo
5' scanning to the initiation codon, with no known role for
complementarity between eukaryotic 18S rRNA and the 5' noncoding
region of mRNAs. We demonstrate that the 5' noncoding region of
human adenovirus late mRNAs, known as the tripartite leader, utilizes a
striking complementarity to 18S rRNA to facilitate a novel form of
translation initiation referred to as ribosome shunting, in which 40S
ribosomes bind the cap and bypass large segments of the mRNA to
reach the initiation codon. Related elements are also shown to promote
ribosome shunting in adenovirus IVa2 intermediate phase
mRNA during virus infection and in human heat shock protein 70 (hsp70) mRNA for selective translation during heat shock.
The importance of mRNA complementarity to 18S rRNA suggests that
ribosome shunting may involve either specific RNA structural features
or a prokaryotic-like interaction between mRNA and rRNA.
[Key Words: Translation; ribosome shunting; adenovirus; hsp70; rRNA]
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