Abstract
Killer strains of the yeast Hanseniaspora uvarum contain cytoplasmic double-stranded RNAs (dsRNAs) of 4.7-kbp L and 1.0-kbp M species, which were shown to be separately packaged into icosahedral virus-like particles exhibiting RNA-dependent RNA polymerase activity. The L genome of the H. uvarum L-dsRNA virion HuV-L was shown to encode a 77-kDa major capsid protein. Peptide maps of the purified HuV coat protein and the 81-kDa major capsid protein from K1 killer viruses of Saccharomyces cerevisiae revealed distinctly different peptide patterns, suggesting significant sequence divergence at the level of the capsid-coding L-dsRNAs. In vitro transcripts from purified HuV-L particles showed no cross-hybridization to denatured L(A), L(B), or L(C), indicating that L from H. uvarum represents a unique L-dsRNA species. Weak, but clearly detectable cross-hybridization of the 1.0-kb dsRNA of HuV-M, encoding the secreted 18-kDa anti-Candida toxin, to the toxin-coding M genomes of S. cerevisiae K1, K2, and K28 killers indicated partial sequence homology among all of the M-dsRNAs tested.
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