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Catalytic RNase P RNA from Synechocystis sp . cleaves the hepatitis C virus RNA near the AUG start codon
Author(s) -
Sabariegos Rosario,
Nadal Anna,
Beguiristain Nerea,
Piron Maria,
Gómez Jordi
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.059
Subject(s) - rnase p , rna , ribozyme , biology , rnase h , microbiology and biotechnology , internal ribosome entry site , ribonuclease , biochemistry , ribosome , virology , chemistry , gene
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.