Information AboutRnase H |
| CATEGORIES ABOUT RNASE H | |
| ribonucleases | |
| ec 3.1.26 | |
| molecular biology | |
|
The Enzyme RNase H () is a Ribonuclease that cleaves the 3'-O-P-bond of RNA in a DNA/RNA Duplex to produce 3'-hydroxyl and 5'-phosphate terminated products. RNase H is a non-specific Endonuclease and catalyzes the cleavage of RNA via an Hydrolytic mechanism, aided by an enzyme-bound divalent metal Ion . In contrast to other Ribonuclease s, such as RNase A or RNase T1 , RNase H leaves a 3'-phosphorylated product. Members of the RNase H family can be found in nearly all organisms, from Archaea and Prokaryota to Eukaryota . In eukaryotic DNA Replication , RNAse H is responsible for cutting out the RNA Primer , allowing completion of the newly synthesized DNA. Retroviral RNase H, a part of the viral Reverse Transcriptase enzyme, is an important pharmaceutical target, as it is absolutely necessary for the proliferation of Retrovirus es, such as HIV . Inhibitors of this enzyme could therefore provide new drugs against diseases like AIDS . As Of 2004 , there are no RNase H inhibitors in clinical trials, though some approaches employing DNA Aptamer s are in the preclinical stage. In a (cDNA) synthesis by Reverse Transcription , as well as procedures such as Nuclease Protection Assay s. RNase H can also be used to degrade specific RNA strands when the cDNA oligo is hybridized, such as the removal of the poly(A) tail from MRNA hybridized to oligo(dT), or the destruction of a chosen Non-coding RNA inside or outside the living cell. To terminate the reaction, a Chelator , such as EDTA , is often added to sequester the required metal ions in the reaction mixture. |
|
|