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Ribosomal proteins mediate the hepatitis C virus IRES–HeLa 40S interaction

Published online by Cambridge University Press:  20 August 2002

GEOFF A. OTTO ,
PETER J. LUKAVSKY ,
ALISSA M. LANCASTER ,
PETER SARNOW  and
JOSEPH D. PUGLISI
GEOFF A. OTTO
Affiliation:
Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California 94305-5126, USA
PETER J. LUKAVSKY
Affiliation:
Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA
ALISSA M. LANCASTER
Affiliation:
Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California 94305-5126, USA
PETER SARNOW
Affiliation:
Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California 94305-5126, USA
JOSEPH D. PUGLISI
Affiliation:
Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA
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Abstract

Translation of the hepatitis C virus genomic RNA is mediated by an internal ribosome entry site (IRES). The 330-nt IRES RNA forms a binary complex with the small 40S ribosomal subunit as a first step in translation initiation. Here chemical probing and 4-thiouridine-mediated crosslinking are used to characterize the interaction of the HCV IRES with the HeLa 40S subunit. No IRES-18S rRNA contacts were detected, but several specific crosslinks to 40S ribosomal proteins were observed. The identity of the crosslinked proteins agrees well with available structural information and provides new insights into HCV IRES function. The protein-rich surface of the 40S subunit thus mediates the IRES–ribosome interaction.

Keywords

eukaryotic translation initiation protein–RNA complexes
Type
Research Article
Information
RNA , Volume 8 , Issue 7 , July 2002 , pp. 913 - 923
Copyright
2002 RNA Society

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