Abstract
RNase H (retroviral ribonuclease H) cleaves the phosphate backbone of the RNA template within an RNA/DNA hybrid to complete the synthesis of double-stranded viral DNA. In the present study we have determined the complete structure of the RNase H domain from XMRV (xenotropic murine leukaemia virus-related virus) RT (reverse transcriptase). The basic protrusion motif of the XMRV RNase H domain is folded as a short helix and an adjacent highly bent loop. Structural superposition and subsequent mutagenesis experiments suggest that the basic protrusion motif plays a role in direct binding to the major groove in RNA/DNA hybrid, as well as in establishing the co-ordination among modules in RT necessary for proper function.
| Original language | English |
|---|---|
| Pages (from-to) | 455-463 |
| Number of pages | 9 |
| Journal | Bioscience Reports |
| Volume | 32 |
| Issue number | 5 |
| DOIs | |
| State | Published - Oct 2012 |
| Externally published | Yes |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Escherichia coli
- Murine leukaemia virus
- Reverse transcriptase
- Ribonuclease H
- Xenotropic murine leukaemia virus-related virus (XMRV)
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