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J. Biol. Chem., Vol. 278, Issue 14, 12231-12240, April 4, 2003
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From the The human La autoantigen has been shown to
interact with the internal ribosome entry site (IRES) of hepatitis C
virus (HCV) in vitro. Using a yeast three-hybrid system, we
demonstrated that, in addition to full-length La protein, both N- and
C-terminal halves were able to interact with HCV IRES in
vivo. The exogenous addition of purified full-length and
truncated La proteins in rabbit reticulocyte lysate showed
dose-dependent stimulation of HCV IRES-mediated
translation. However, an additive effect was achieved adding the
terminal halves together in the reaction, suggesting that both might
play critical roles in achieving full stimulatory activity of the
full-length La protein. Using computational analysis, three-dimensional
structures of the RNA recognition motifs (RRM) of the La protein were
independently modeled. Of the three putative RRMs, RRM2 was predicted
to have a good binding pocket for the interaction with the HCV IRES
around the GCAC motif near the initiator AUG and RRM3 binds perhaps in
a different location. This observation was further investigated by the
filter-binding and toe-printing assays. The results presented here
strongly suggest that both the N- and C-terminal halves can interact
independently with the HCV IRES and are involved in stimulating
internal initiation of translation.
Hepatitis C Virus Internal Ribosome Entry Site-mediated
Translation Is Stimulated by Specific Interaction of Independent
Regions of Human La Autoantigen*
§,
,
Department of Microbiology and Cell Biology
and the ¶ Molecular Biophysics Unit, Indian Institute of Science,
Bangalore 560012, India
*
This work was supported in part by a grant from the
Department of Science and Technology, India (to S. D.).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.
Supported by a Wellcome Trust grant.
**
International Senior Fellow of the Wellcome Trust.
To whom correspondence should be addressed. Tel.:
91-80-394-2886; Fax: 91-80-360-2697; E-mail:
sdas@mcbl.iisc.ernet.in.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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