Ty3 reverse transcriptase complexed with an RNA-DNA hybrid shows structural and functional asymmetry
| Autor: | Jakub Jurkowski, Jennifer T. Miller, Roman H. Szczepanowski, Justyna Studnicka, Stuart F.J. Le Grice, Marcin Nowotny, Elzbieta Nowak, Marion K. Bona |
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| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Binding Sites Saccharomyces cerevisiae Proteins Retroelements biology DNA polymerase Ribonuclease H food and beverages Substrate (chemistry) RNA-Directed DNA Polymerase Retrotransposon DNA Crystallography X-Ray Molecular biology Article Reverse transcriptase Protein Structure Tertiary Structural Biology biology.protein Transferase Functional asymmetry RNase H Dimerization Molecular Biology |
| Zdroj: | Nature structural & molecular biology |
| ISSN: | 1545-9985 1545-9993 |
| Popis: | 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). However, while 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. More strikingly, our structure and biochemical data suggest that the RNase H and DNA polymerase activities are contributed by individual subunits of the homodimer. |
| Databáze: | OpenAIRE |
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