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J. Biol. Chem., Vol. 276, Issue 24, 20824-20826, June 15, 2001

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ACCELERATED PUBLICATION
Ribosomal Protein S5 Interacts with the Internal Ribosomal Entry Site of Hepatitis C Virus^*

Shuetsu Fukushi^§, Masato Okada^¶, Joachim Stahl, Tsutomu Kageyama, Fuminori B. Hoshino, and Kazuhiko Katayama

From the  Research and Development Center, BioMedical Laboratories, 1361-1 Matoba, Kawagoe, Saitama 350-1101, Japan, the ^¶ Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan, and the  Max-Delbrück Center for Molecular Medicine, D-13125 Berlin-Buch, Germany

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.

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