Catalytic RNase P RNA from Synechocystis sp. cleaves the hepatitis C virus RNA near the AUG start codon.
Previously, we described two RNA structural motifs in the hepatitis C viral (HCV) genome that can be processed in vitro by human ribonuclease P (RNase P) enzyme [J. Biol. Chem. 277 (2002) 30606]. One of these structures is located in the internal ribosome entry site and is conserved in the related animal pestiviruses [J. Biol. Chem. 278 (2003) 26844]. Here, we tested two prokaryotic RNase P ribozymes (P RNA) against this conserved structural motif. In vitro experiments indicated that P RNA from Synechocystis sp. can specifically process the viral transcript preparations in a position close to the human RNase P cleavage site. This provides additional support for the presence of an RNA structure similar to tRNA near the AUG start codon and suggests that Synechocystis P RNA may be an active agent for HCV antigenomic interventions.
Sabariegos
Rosario
R
Servicio de Medicina Interna-Hospital Vall d'Hebron, Area de Investigación Básica, Barcelona 08035, Spain.
Nadal
Anna
A
Beguiristain
Nerea
N
Piron
Maria
M
Gómez
Jordi
J
D001345:Autoradiography; D001483:Base Sequence; D001665:Binding Sites; D002384:Catalysis; D018387:Codon, Initiator / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D014644:Genetic Variation; D016174:Hepacivirus / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D009690:Nucleic Acid Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016337:RNA, Catalytic / Q000378:metabolism; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D043262:Ribonuclease P / Q000378:metabolism*; D046939:Synechocystis / Q000201:enzymology*
D018387:Codon, Initiator; D016337:RNA, Catalytic; D012367:RNA, Viral; D043262:Ribonuclease P