Characterizing the functions of Ty1 Gag and the Gag-derived restriction factor p22/p18

References

• Curcio MJ, Lutz S, Lesage P. The Ty1 LTR-retrotransposon of budding yeast. Microbiol Spectr 2015; 3:1-35; PMID:25893143
   PubMed Web of Science ®Google Scholar
• Belcourt MF, Farabaugh PJ. Ribosomal frameshifting in the yeast retrotransposon Ty: tRNAs induce slippage on a 7 nucleotide minimal site. Cell 1990; 62:339-52; PMID:2164889; http://dx.doi.org/10.1016/0092-8674(90)90371-K
   PubMed Web of Science ®Google Scholar
• Malagon F, Jensen TH. The T body, a new cytoplasmic RNA granule in Saccharomyces cerevisiae. Mol Cell Biol 2008; 28:6022-32; PMID:18678648; http://dx.doi.org/10.1128/MCB.00684-08
   PubMed Web of Science ®Google Scholar
• Malagon F, Jensen TH. T-body formation precedes virus-like particle maturation in S. cerevisiae. RNA Biol 2011; 8:184-9; PMID:21358276; http://dx.doi.org/10.4161/rna.8.2.14822
   PubMed Web of Science ®Google Scholar
• Feng YX, Moore SP, Garfinkel DJ, Rein A. The genomic RNA in Ty1 virus-like particles is dimeric. J Virol 2000; 74:10819-21; PMID:11044130; http://dx.doi.org/10.1128/JVI.74.22.10819-10821.2000
   PubMed Web of Science ®Google Scholar
• Keeney JB, Chapman KB, Lauermann V, Voytas DF, Aström SU, von Pawel-Rammingen U, Bystrom A, Boeke JD. Multiple molecular determinants for retrotransposition in a primer tRNA. Mol Cell Biol 1995; 15:217-26; PMID:7528326; http://dx.doi.org/10.1128/MCB.15.1.217
   PubMed Web of Science ®Google Scholar
• Devine SE, Boeke JD. Integration of the yeast retrotransposon Ty1 is targeted to regions upstream of genes transcribed by RNA polymerase III. Genes Dev 1996; 10:620-33; PMID:8598291; http://dx.doi.org/10.1101/gad.10.5.620
   PubMed Web of Science ®Google Scholar
• Huang CR, Burns KH, Boeke JD. Active transposition in genomes. Annu Rev Genet 2012; 46:651-75; PMID:23145912; http://dx.doi.org/10.1146/annurev-genet-110711-155616
   PubMed Web of Science ®Google Scholar
• Babatz TD, Burns KH. Functional impact of the human mobilome. Curr Opin Genet Dev 2013; 23:264-70; PMID:23523050; http://dx.doi.org/10.1016/j.gde.2013.02.007
   PubMed Web of Science ®Google Scholar
• Kazazian HH, Jr. Mobile elements: drivers of genome evolution. Science 2004; 303:1626-32; PMID:15016989; http://dx.doi.org/10.1126/science.1089670
   PubMed Web of Science ®Google Scholar
• Slotkin RK, Martienssen R. Transposable elements and the epigenetic regulation of the genome. Nat Rev Genet 2007; 8:272-85; PMID:17363976; http://dx.doi.org/10.1038/nrg2072
   PubMed Web of Science ®Google Scholar
• Drinnenberg IA, Fink GR, Bartel DP. Compatibility with killer explains the rise of RNAi-deficient fungi. Science 2011; 333:1592; PMID:21921191; http://dx.doi.org/10.1126/science.1209575
   PubMed Web of Science ®Google Scholar
• Garfinkel DJ, Nyswaner K, Wang J, Cho JY. Post-transcriptional cosuppression of Ty1 retrotransposition. Genetics 2003; 165:83-99; PMID:14504219
   PubMed Web of Science ®Google Scholar
• Saha A, Mitchell JA, Nishida Y, Hildreth JE, Ariberre JA, Gilbert WA, Garfinkel DJ. A trans-dominant form of Gag restricts Ty1 retrotransposition and mediates copy number control. J Virol 2015; 89:3922-38; PMID:25609815; http://dx.doi.org/10.1128/JVI.03060-14
   PubMed Web of Science ®Google Scholar
• Garfinkel DJ, Tucker JM, Saha A, Nishida Y, Pachulska-Wieczorek K, Blaszczyk L, Purzycka KJ. A self-encoded capsid derivative restricts Ty1 retrotransposition in Saccharomyces. Curr Genet 2015; PMID:26650614.
   PubMedGoogle Scholar
• Nishida Y, Pachulska-Wieczorek K, Blaszczyk L, Saha A, Gumna J, Garfinkel DJ, Purzycka KJ. Ty1 retrovirus-like element Gag contains overlapping restriction factor and nucleic acid chaperone functions. Nucleic Acids Res 2015; 43:7414-31; PMID:26160887; http://dx.doi.org/10.1093/nar/gkv695
   PubMed Web of Science ®Google Scholar
• Cristofari G, Ficheux D, Darlix JL. The GAG-like protein of the yeast Ty1 retrotransposon contains a nucleic acid chaperone domain analogous to retroviral nucleocapsid proteins. J Biol Chem 2000; 275:19210-7; PMID:10766747; http://dx.doi.org/10.1074/jbc.M001371200
   PubMed Web of Science ®Google Scholar
• Pachulska-Wieczorek K, Stefaniak AK, Purzycka KJ. Similarities and differences in the nucleic acid chaperone activity of HIV-2 and HIV-1 nucleocapsid proteins in vitro. Retrovirology 2014; 11:54; PMID:24992971; http://dx.doi.org/10.1186/1742-4690-11-54
   PubMed Web of Science ®Google Scholar
• Huang Q, Purzycka KJ, Lusvarghi S, Li D, Legrice SF, Boeke JD. Retrotransposon Ty1 RNA contains a 5′-terminal long-range pseudoknot required for efficient reverse transcription. RNA 2013; 19:320-32; PMID:23329695; http://dx.doi.org/10.1261/rna.035535.112
   PubMed Web of Science ®Google Scholar
• Purzycka KJ, Legiewicz M, Matsuda E, Eizentstat LD, Lusvarghi S, Saha A, Le Grice SF, Garfinkel DJ. Exploring Ty1 retrotransposon RNA structure within virus-like particles. Nucleic Acids Res 2013; 41:463-73; PMID:23093595; http://dx.doi.org/10.1093/nar/gks983
   PubMed Web of Science ®Google Scholar
• Purzycka KJ, Garfinkel DJ, Boeke JD, Le Grice SF. Influence of RNA structural elements on Ty1 retrotransposition. Mob Genet Elements 2013; 3:e25060; PMID:23914314; http://dx.doi.org/10.4161/mge.25060
   PubMedGoogle Scholar
• Johnson SF, Telesnitsky A. Retroviral RNA dimerization and packaging: the what, how, when, where, and why. PLoS Pathog 2010; 6:e1001007; PMID:20949075; http://dx.doi.org/10.1371/journal.ppat.1001007
   PubMed Web of Science ®Google Scholar
• Dutko JA, Kenny AE, Gamache ER, Curcio MJ. 5′ to 3′ mRNA decay factors colocalize with Ty1 gag and human APOBEC3G and promote Ty1 retrotransposition. J Virol 2010; 84:5052-66; PMID:20219921; http://dx.doi.org/10.1128/JVI.02477-09
   PubMed Web of Science ®Google Scholar
• Tucker JM, Larango ME, Wachsmuth LP, Kannan N, Garfinkel DJ. The Ty1 Retrotransposon Restriction Factor p22 Targets Gag. PLoS Genet 2015; 11:e1005571; PMID:26451601; http://dx.doi.org/10.1371/journal.pgen.1005571
   PubMed Web of Science ®Google Scholar