What is the Difference Between RNASE A and RNASE H?

The main difference between RNase A and RNase H lies in their mode of action and specificity. Here are the key differences:

1. Specificity: RNase A is a pancreatic ribonuclease that specifically cleaves the 3' end of unpaired cytosine and uracil residues in single-stranded RNA. On the other hand, RNase H is a nonspecific ribonuclease enzyme that degrades RNA in RNA-DNA hybrids via hydrolytic reactions.
2. Nature of RNA Cleaving: RNase A cleaves single-stranded RNA at higher salt concentrations, while RNase H cleaves RNA in RNA-DNA hybrids.
3. Co-factors for Activity: RNase A does not need cofactors for its activity, whereas RNase H requires metal ions as cofactors for its function.

Both RNase A and RNase H are endoribonucleases, but they have distinct roles and mechanisms of action. RNase A is mainly used for breaking down RNA molecules, while RNase H is involved in the degradation of RNA in RNA-DNA hybrids, making it useful for removing poly-A tails from mRNA and other applications.

Comparative Table: RNASE A vs RNASE H

Here is a table comparing the differences between RNase A and RNase H:

RNase A is a popular enzyme in molecular research and is extracted from bovine pancreas. It is an endoribonuclease that hydrolyzes phosphodiester bonds on the 3' side of pyrimidic nucleotides C and U of single-stranded RNA. On the other hand, RNase H is a nonspecific ribonuclease enzyme that degrades RNA in RNA-DNA hybrids via hydrolytic reactions. It is involved in removing poly-A tails from mRNA hybridized to oligo (dt) and is used in RNA template removal during complementary DNA synthesis.