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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.

Author information

1
Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, Warsaw, Poland.
2
Reverse Transcriptase Biochemistry Section, HIV Drug Resistance Program, Frederick National Laboratory, Frederick, Maryland, USA.
3
Biophysics Core Facility, International Institute of Molecular and Cell Biology, Warsaw, Poland.

Abstract

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.

PMID:
24608367
DOI:
10.1038/nsmb.2785
[Indexed for MEDLINE]

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