Abstract
RNA-DNA hybrids play essential roles in a variety of biological processes, including DNA replication, transcription, and viral integration. Ribonucleotides incorporated within DNA are hydrolyzed by RNase H enzymes in a removal process that is necessary for maintaining genomic stability. In order to understand the structural determinants involved in recognition of a hybrid substrate by RNase H we have determined the crystal structure of a dodecameric nonpolypurine/ polypyrimidine tract RNA-DNA duplex. A comparison to the same sequence bound to RNase H, reveals structural changes to the duplex that include widening of the major groove to 12.5 A from 4.2 Å and decreasing the degree of bending along the axis which may play a crucial role in the ribonucleotide recognition and cleavage mechanism within RNase H. This structure allows a direct comparison to be made about the conformational changes induced in RNA-DNA hybrids upon binding to RNase H and may provide insight into how dysfunction in the endonuclease causes disease.
Original language | English (US) |
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Pages (from-to) | 668-673 |
Number of pages | 6 |
Journal | Cell Cycle |
Volume | 14 |
Issue number | 4 |
DOIs | |
State | Published - Feb 15 2015 |
Bibliographical note
Publisher Copyright:© 2015 Taylor & Francis Group, LLC.
Keywords
- Conformational changes
- Protein nucleic acid interaction
- RNA-DNA hybrid
- RNase H