Ribosomal protein S5 interacts with the internal ribosomal entry site of hepatitis C virus

Item Type:	Article
Title:	Ribosomal protein S5 interacts with the internal ribosomal entry site of hepatitis C virus
Creators Name:	Fukushi, S. and Okada, M. and Stahl, J. and Kageyama, T. and Hoshino, F.B. and Katayama, K.
Abstract:	Translational initiation of hepatitis C virus (HCV) genome RNA occurs via its highly structured 5′ noncoding region called the internal ribosome entry site (IRES). Recent studies indicate that HCV IRES and 40 S ribosomal subunit form a stable binary complex that is believed to be important for the subsequent assembly of the 48 S initiation complex. Ribosomal protein (rp) S9 has been suggested as the prime candidate protein for binding of the HCV IRES to the 40 S subunit. RpS9 has a molecular mass of ∼25 kDa in UV cross-linking experiments. In the present study, we examined the ∼25-kDa proteins of the 40 S ribosome that form complexes with the HCV IRES upon UV cross-linking. Immunoprecipitation with specific antibodies against two 25-kDa 40 S proteins, rpS5 and rpS9, clearly identified rpS5 as the protein bound to the IRES. Thus, our results support rpS5 as the critical element in positioning the HCV RNA on the 40 S ribosomal subunit during translation initiation.
Source:	Journal of Biological Chemistry
ISSN:	0021-9258
Publisher:	American Society for Biochemistry and Molecular Biology
Volume:	276
Number:	24
Page Range:	20824-20826
Date:	1 January 2001
Official Publication:	https://doi.org/10.1074/jbc.C100206200
PubMed:	View item in PubMed

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