Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes.
All organisms studied contain many RNases of many different classes, showing that RNA degradation is a very ancient and important process. As well as cleaning of cellular RNA that is no longer required, RNases play key roles in the maturation of all RNA molecules, both messenger RNAs that carry genetic material for making proteins, and non-coding RNAs that function in varied cellular processes. In addition, active RNA degradation systems are a first defense against RNA viruses, and provide the underlying machinery for more advanced cellular immune strategies such as RNAi.
Some cells also secrete copious quantities of non-specific RNases such as A and T1. RNases are, therefore, extremely common, resulting in very short lifespans for any RNA that is not in a protected environment. It is worth noting that all intracellular RNAs are protected from RNase activity by a number of strategies including 5' end capping, 3' end polyadenylation, and folding within an RNA protein complex (ribonucleoprotein particle or RNP).
Ribonuclease (poly-(U)-specific) (EC 3.1.26.9, ribonuclease (uracil-specific), uracil-specific endoribonuclease, uracil-specific RNase) is an enzyme. This enzyme catalyses the following chemical reaction
This enzyme forms oligonucleotides with chain lengths of 6 to 12.
Ribonuclease U2 (EC 3.1.27.4, purine specific endoribonuclease, ribonuclease U3, RNase U3, RNase U2, purine-specific ribonuclease, purine-specific RNase, Pleospora RNase, Trichoderma koningi RNase III, ribonuclease (purine)) is an enzyme. This enzyme catalyses the following chemical reaction