Structure of Ty1 Internally Initiated RNA Influences Restriction Factor Expression
| Autor: | Katarzyna J. Purzycka, Leszek Błaszczyk, David J. Garfinkel, Marcin Biesiada, Agniva Saha |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Retroelements viruses lcsh:QR1-502 Gene Products gag RNA-dependent RNA polymerase Saccharomyces cerevisiae translation regulation Biology lcsh:Microbiology Article 03 medical and health sciences Virology RNA structure Gag Recombination Genetic Genetics Intron RNA RNA Fungal Non-coding RNA Post-transcriptional modification RNA silencing 030104 developmental biology Infectious Diseases RNA editing Protein Biosynthesis Ty1 retrotransposon Small nuclear RNA |
| Zdroj: | Viruses Viruses; Volume 9; Issue 4; Pages: 74 Viruses, Vol 9, Iss 4, p 74 (2017) |
| ISSN: | 1999-4915 |
| DOI: | 10.3390/v9040074 |
| Popis: | The long-terminal repeat retrotransposon Ty1 is the most abundant mobile genetic element in many Saccharomyces cerevisiae isolates. Ty1 retrotransposons contribute to the genetic diversity of host cells, but they can also act as an insertional mutagen and cause genetic instability. Interestingly, retrotransposition occurs at a low level despite a high level of Ty1 RNA, even though S. cerevisiae lacks the intrinsic defense mechanisms that other eukaryotes use to prevent transposon movement. p22 is a recently discovered Ty1 protein that inhibits retrotransposition in a dose-dependent manner. p22 is a truncated form of Gag encoded by internally initiated Ty1i RNA that contains two closely-spaced AUG codons. Mutations of either AUG codon compromise p22 translation. We found that both AUG codons were utilized and that translation efficiency depended on the Ty1i RNA structure. Structural features that stimulated p22 translation were context dependent and present only in Ty1i RNA. Destabilization of the 5′ untranslated region (5′ UTR) of Ty1i RNA decreased the p22 level, both in vitro and in vivo. Our data suggest that protein factors such as Gag could contribute to the stability and translational activity of Ty1i RNA through specific interactions with structural motifs in the RNA. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|