Abstract:
:Hepatitis C virus (HCV) non-structural protein 5B (NS5B) is an RNA replicase. We expressed full-length NS5B (591 amino acid residues) in Escherichia coli as a fusion protein with maltose binding protein (MBP-NS5B). MBP-NS5B was recovered in the soluble fraction after centrifugation at 40,000 x g and affinity-purified with amylose resin. The purified MBP-NS5B had a high-level of poly (A), oligo (U)-dependent UMP incorporation with a Km of 2 microM for UTP. Surprisingly, the enzymatically active MBP-NS5B was sedimented by ultracentrifugation at 160,000 x g. The pellet contained 16S and 23S ribosomal RNAs, suggesting that ribosomes were associated with MBP-NS5B. Ribosomes and MBP-NS5B were subsequently co-purified on amylose resin. Deletion study revealed that either the N-terminal (amino acid residues 1-107) or the C-terminal (amino acid residues 498-591) region of NS5B were sufficient for this association with ribosomes. We further found that NS5B also bound with human ribosomes. Our results implicate a novel mechanism of coupling between replication and translation of the viral genome in the life cycle of HCV.
journal_name
Microbiol Immunoljournal_title
Microbiology and immunologyauthors
Tanaka T,Sugiyama K,Ikeda M,Naganuma A,Nozaki A,Saito M,Shimotohno K,Kato Ndoi
10.1111/j.1348-0421.2000.tb02532.xkeywords:
subject
Has Abstractpub_date
2000-01-01 00:00:00pages
543-50issue
6eissn
0385-5600issn
1348-0421journal_volume
44pub_type
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