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Ribonuclease L or RNase L (for latent), known sometimes as ribonuclease 4 or 2'-5' oligoadenylate synthetase-dependent ribonuclease, is an interferon (IFN)-induced ribonuclease which, upon activation, destroys all RNA within the cell (both cellular and viral) as well as inhibiting mRNA export.
RNase L is an interferon-induced nuclease that, upon activation, destroys all RNA within the cell EC 3.1.26.5 : RNase P is a type of ribonuclease that is unique in that it is a ribozyme – a ribonucleic acid that acts as a catalyst in the same way as an enzyme .
Ribonuclease L normally binds to 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) and inhibits the interferon-regulated 2-5A/RNase L pathway, which is used by viruses. ABCE1 heterodimerize with ribonuclease L and prevents its interaction with 2-5A, antagonizing the anti-viral properties of ribonuclease L, [ 6 ] and allow the virus to ...
Bovine pancreatic ribonuclease is the best-studied member of the family and has served as a model system in work related to protein folding, disulfide bond formation, protein crystallography and spectroscopy, and protein dynamics. [2]
The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'-5'-oligoadenylates, which activate latent ribonuclease (RNase-L), resulting in degradation of viral RNA and inhibition of virus replication. [1]
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Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase, is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides. [1] [2] It catalyzes this formation by removing the 2'-hydroxyl group of the ribose ring of nucleoside diphosphates (or triphosphates depending on the class of RNR).