Everything about Rnase H totally explained
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.
Members of the RNase H family can be found in nearly all organisms, from
archaea and
prokaryota to
eukaryota. In
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's absolutely necessary for the proliferation of
retroviruses, 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
aptamers are in the preclinical stage.
In a
molecular biology laboratory, as RNase H specifically degrades the RNA in RNA:DNA hybrids and won't degrade DNA or unhybridized RNA, it's commonly used to destroy the RNA template after first-strand
complementary DNA (cDNA) synthesis by
reverse transcription, as well as procedures such as
nuclease protection assays. 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.
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