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Abstract

Transposable elements are selfish mobile genetic elements able to replicate in the host genome and are classified as either DNA type elements or retrotransposons. In our study, we focus on R2 retrotransposable elements. Retrotransposable elements can reverse transcribe an RNA intermediate into DNA either before or during integration into the target genome. The R2 element exclusively inserts in the 28S rRNA genes via the mechanism of target primed reverse transcription (TPRT). For the TPRT mechanism to occur, the 5' and 3' ends of the RNA intermediate must bind to R2 protein before cleavage and insertion into a new genomic site can occur. Despite its importance in TPRT, RNA binding sequences of the R2 protein are not well understood. The objective of this study was to create single alanine replacements via site-directed mutagenesis in both the RYGLV and KPQQR sequences, which are highly conserved in the thumb domain of the R2 protein, and to isolate this mutated R2 protein for use in future assays. By examining the RNA binding properties of the R2 protein, we can further understand the TPRT mechanism and its overall role in retrotransposon success.

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