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Publication Abstract from PubMed

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 non-polypurine/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 A 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.

Crystal structure of RNA-DNA duplex provides insight into conformational changes induced by RNase H binding.,Davis RR, Shaban NM, Perrino FW, Hollis T Cell Cycle. 2015 Feb 16;14(4):668-73. doi: 10.4161/15384101.2014.994996. PMID:25664393^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.