| Ribonuclease | |||||||||||
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| Identifiers | |||||||||||
| Symbol | Ribonuclease | ||||||||||
| Pfam | PF00545 | ||||||||||
| InterPro | IPR000026 | ||||||||||
| SCOP2 | 1brn / SCOPe / SUPFAM | ||||||||||
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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.
Ribonucleases are found in all domains of life as well as in viruses. While some families of RNases, such as EndoU-like RNases, are ubiquitous, others, such as RNase A, are only found in a subset of vertebrates. [2] RNases play a role in a multitude of processes including antiviral defense, mRNA regulation, RNA maturation of coding and noncoding RNA, RNA interference and replication in retroviruses. [3]
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. All intracellular RNAs are protected from RNase activity by a number of strategies including 5' end capping, 3' end polyadenylation, formation of an RNA·RNA duplex, and folding within an RNA protein complex (ribonucleoprotein particle or RNP).[ citation needed ]
Another mechanism of protection is ribonuclease inhibitor (RI), which binds to certain ribonucleases with the highest affinity of any protein-protein interaction; the dissociation constant for the RI-RNase A complex is between 10-14 and 10-16 M under physiological conditions. [4] Recombinant RNase inhibitors (RRIs), which are in-vitro synthesized RI, are used in most laboratories that study RNA to protect their samples against degradation from environmental RNases. [5]
Similar to restriction enzymes, which cleave highly specific sequences of double-stranded DNA, a variety of endoribonucleases that recognize and cleave specific sequences of single-stranded RNA have been recently classified. [6]
RNases play a critical role in many biological processes, including angiogenesis and self-incompatibility in flowering plants (angiosperms). [7] [8] Many stress-response toxins of prokaryotic toxin-antitoxin systems have been shown to have RNase activity and homology. [9]
The active site looks like a rift valley where all the active site residues create the wall and bottom of the valley. The rift is very thin and the small substrate fits perfectly in the middle of the active site, which allows for perfect interaction with the residues. It actually has a little curvature to the site which the substrate also has. Although usually most exo- and endoribonucleases are not sequence specific, recently CRISPR/Cas system natively recognizing and cutting DNA was engineered to cleave ssRNA in a sequence-specific manner. [17]
The extraction of RNA in molecular biology experiments is greatly complicated by the presence of ubiquitous and hardy ribonucleases that degrade RNA samples. Certain RNases can be extremely hardy and inactivating them is difficult compared to neutralizing DNases. In addition to the cellular RNases that are released, there are several RNases that are present in the environment. RNases have evolved to have many extracellular functions in various organisms. [18] [19] [20] For example, RNase 7, a member of the RNase A superfamily, is secreted by human skin and serves as a potent antipathogen defence. [21] [22] In these secreted RNases, the enzymatic RNase activity may not even be necessary for its new, exapted function. For example, immune RNases act by destabilizing the cell membranes of bacteria. [23] [24]
