Ribosomal protein and biogenesis factors affect multiple steps during movement of the Saccharomyces cerevisiae Ty1 retrotransposon. Issue 1 (December 2015)

• Record Type: Journal Article
• Authors: Suresh, Susmitha; Ahn, Hyo; Joshi, Kartikeya; Dakshinamurthy, Arun; Kananganat, Arun; Garfinkel, David; Farabaugh, Philip
• Is Part Of: Mobile DNA. Volume 6:Issue 1(2015)
• Page Start: 1
• Page End: 14
• Publication Date: 2015-12
• Subjects: Retrotransposition -- Host factors -- Programmed frameshifting -- Ribosomal protein insufficiency -- Ribosome biogenesis; Mobile genetic elements -- Periodicals; Genomics -- Periodicals; 572.869
• DOI: 10.1186/s13100-015-0053-5
• Languages: English
• ISSNs: 1759-8753

Abstract

Abstract Background A large number ofSaccharomyces cerevisiae cellular factors modulate the movement of the retrovirus-like transposon Ty1. Surprisingly, a significant number of chromosomal genes required for Ty1 transposition encode components of the translational machinery, including ribosomal proteins, ribosomal biogenesis factors, protein trafficking proteins and protein or RNA modification enzymes. Results To assess the mechanistic connection between Ty1 mobility and the translation machinery, we have determined the effect of these mutations on ribosome biogenesis and Ty1 transcriptional and post-transcriptional regulation. Lack of genes encoding ribosomal proteins or ribosome assembly factors causes reduced accumulation of the ribosomal subunit with which they are associated. In addition, these mutations cause decreased Ty1 + 1 programmed translational frameshifting, and reduced Gag protein accumulation despite at least normal levels of Ty1 mRNA. Several ribosome subunit mutations increase the level of both an internally initiated Ty1 transcript and its encoded truncated Gag-p22 protein, which inhibits transposition. Conclusions Together, our results suggest that this large class of cellular genes modulate Ty1 transposition through multiple pathways. The effects are largely post-transcriptional acting at a variety of levels that may include translation initiation, protein stability and subcellular protein localization.