The double-stranded RNA genome of yeast virus L-A encodes its own putative RNA polymerase by fusing two open reading frames.
作者： T Icho , R B Wickner
DOI: 10.1016/S0021-9258(18)83488-3
关键词: Genetics 、 RNA editing 、 Molecular biology 、 RNA-dependent RNA polymerase 、 Ribosomal frameshift 、 Non-coding RNA 、 RNA virus 、 Totivirus 、 Biology 、 Intron 、 RNA
摘要: Abstract The L-A double-stranded RNA virus of Saccharomyces cerevisiae encodes its major coat protein (80 kDa) and a minor single-stranded binding (180 that has immunological cross-reactivity with the protein. sequence cDNA clones revealed two open reading frames (ORF), ORF1 ORF2. These overlap by 130 base pairs ORF2 is in -1 frame respect to ORF1. Although viral particles encoded ORF1, 180-kDa derived from entire genome fusing ORF2, probably translational frameshift. Within overlapping region similar producing frameshift "simultaneous slippage" retroviruses. coding shows pattern characteristic RNA-dependent polymerases icosahedral (+)-strand viruses. Thus, analogous gag-pol fusion proteins.
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