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Exploring Ty1 retrotransposon RNA structure within virus-like particles.


ABSTRACT: Ty1, a long terminal repeat retrotransposon of Saccharomyces, is structurally and functionally related to retroviruses. However, a differentiating aspect between these retroelements is the diversity of the replication strategies used by long terminal repeat retrotransposons. To understand the structural organization of cis-acting elements present on Ty1 genomic RNA from the GAG region that control reverse transcription, we applied chemoenzymatic probing to RNA/tRNA complexes assembled in vitro and to the RNA in virus-like particles. By comparing different RNA states, our analyses provide a comprehensive structure of the primer-binding site, a novel pseudoknot adjacent to the primer-binding sites, three regions containing palindromic sequences that may be involved in RNA dimerization or packaging and candidate protein interaction sites. In addition, we determined the impact of a novel form of transposon control based on Ty1 antisense transcripts that associate with virus-like particles. Our results support the idea that antisense RNAs inhibit retrotransposition by targeting Ty1 protein function rather than annealing with the RNA genome.

SUBMITTER: Purzycka KJ 

PROVIDER: S-EPMC3592414 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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Exploring Ty1 retrotransposon RNA structure within virus-like particles.

Purzycka Katarzyna J KJ   Legiewicz Michal M   Matsuda Emiko E   Eizentstat Linda D LD   Lusvarghi Sabrina S   Saha Agniva A   Le Grice Stuart F J SF   Garfinkel David J DJ  

Nucleic acids research 20121023 1


Ty1, a long terminal repeat retrotransposon of Saccharomyces, is structurally and functionally related to retroviruses. However, a differentiating aspect between these retroelements is the diversity of the replication strategies used by long terminal repeat retrotransposons. To understand the structural organization of cis-acting elements present on Ty1 genomic RNA from the GAG region that control reverse transcription, we applied chemoenzymatic probing to RNA/tRNA complexes assembled in vitro a  ...[more]

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