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   <subfield code="a">Identification of a Ribosomal Frameshift in Leishmania RNA Virus 1-4</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Sang Eun Lee, Jae Myoung Suh, Scott Scheffter, Jean L. Patterson, In Kwon Chung]</subfield>
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   <subfield code="a">Double-stranded Leishmania RNA virus 1-4 (LRV 1-4) has at least four open reading frames (ORFs). The two small ORFs located near its 5′ terminus, ORF1 and ORFx, could encode 34- and 60-amino acid polypeptides, respectively. ORF2 encodes an 82-kDa major capsid protein, and 0RF3 encodes a 98-kDa polypeptide which contains the consensus sequence for RNA-dependent RNA polymerases of plus-strand and double-stranded RNA viruses. The complete sequence of LRV 1-4 shows that 0RF2 and ORF3 overlap by 71 nucleotides, and that 0RF3 lacks a potential translation initiation site, suggesting that the viral polymerase may be synthesized as a 180-kDa fusion protein with the virus capsid. In this report, we present evidence for the synthesis of a fusion protein through a ribosomal frameshift. In vitro-translation experiments and immunostudies involving antiserum against the viral capsid protein demonstrated that the overlapping 71 nucleotides of ORF2 and 0RF3 are contained in a region which promotes translational frameshifting. Computer analysis of the putative frameshift region revealed a potential pseudoknot structure located within the overlapping 71 nucleotide sequence.</subfield>
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   <subfield code="t">The Journal of Biochemistry</subfield>
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