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Nat Struct Mol Biol. 2014 Apr;21(4):389-96. doi: 10.1038/nsmb.2785. Epub 2014 Mar 9.

Ty3 reverse transcriptase complexed with an RNA-DNA hybrid shows structural and functional asymmetry.

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Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, Warsaw, Poland.
Reverse Transcriptase Biochemistry Section, HIV Drug Resistance Program, Frederick National Laboratory, Frederick, Maryland, USA.
Biophysics Core Facility, International Institute of Molecular and Cell Biology, Warsaw, Poland.


Retrotransposons are a class of mobile genetic elements that replicate by converting their single-stranded RNA intermediate to double-stranded DNA through the combined DNA polymerase and ribonuclease H (RNase H) activities of the element-encoded reverse transcriptase (RT). Although a wealth of structural information is available for lentiviral and gammaretroviral RTs, equivalent studies on counterpart enzymes of long terminal repeat (LTR)-containing retrotransposons, from which they are evolutionarily derived, is lacking. In this study, we report the first crystal structure of a complex of RT from the Saccharomyces cerevisiae LTR retrotransposon Ty3 in the presence of its polypurine tract-containing RNA-DNA hybrid. In contrast to its retroviral counterparts, Ty3 RT adopts an asymmetric homodimeric architecture whose assembly is substrate dependent. Moreover, our structure and biochemical data suggest that the RNase H and DNA polymerase activities are contributed by individual subunits of the homodimer.

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