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J. Biol. Chem., Vol. 276, Issue 45, 41648-41655, November 9, 2001
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From the International Centre for Genetic Engineering and
Biotechnology, 34012 Trieste, Italy
The hepatitis C virus (HCV) 5'-untranslated
region and, in particular, domains II to IV are involved in the
internal ribosome entry site (IRES) structure. Recent structural
evidence has shown that the function of domain II may be to hold the
coding RNA in position until the translational machinery is correctly
assembled on the decoding site. However, a comprehensive mutational and functional study concerning the importance of the different RNA regions
that compose domain II is not yet available. Therefore, we have taken
advantage of the recently proposed secondary structure of domain II to
design a series of specific mutants. The bulge regions present in the
latest secondary structure prediction of domain II were selectively
deleted, and the effects of these mutations on IRES translation
efficiency were analyzed. Our results show that the introduction of
these mutations can variably affect the degree of HCV
translation, causing a moderate to total loss of translation ability
that correlates with the severity of changes induced in the RNA
secondary structure and degree of p25 ribosomal protein UV
cross-linking, but not with the ability of the 40S ribosomal subunit to
bind the IRES. These findings support the proposed structural
role of domain II in HCV translation.
Mutational Analysis of the Different Bulge Regions of Hepatitis C
Virus Domain II and Their Influence on Internal Ribosome Entry Site
Translational Ability*
, and
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: International Centre
for Genetic Engineering and Biotechnology, Padriciano 99, 34012 Trieste, Italy. Tel.: 39-40-3757337; Fax: 39-40-3757361; E-mail:
baralle@icgeb.trieste.it.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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