Ribonuclease
From Free net encyclopedia
Ribonuclease, abbreviated commonly as RNase, is an enzyme that catalyzes the breakdown of RNA into smaller components.
RNAses are extremely common in the modern world, resulting in very short lifespans for any RNA that is not in a protected environment.
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Major types
- RNase A is an RNase that is commonly used in research. RNase A (e.g., bovine pancreatic ribonuclease A: Template:PDB, Template:EC number) is one of the hardiest enzymes in common laboratory usage; one method of isolating it is to boil a crude cellular extract until all enzymes other than RNase A are denatured.
- RNase P is a type of ribonuclease and is currently under heavy research. RNase P is unique from other RNases in that it is a ribozyme – a ribonucleic acid that acts as a catalyst in the same way that a protein based enzyme would. Its function is to cleave off an extra, or precursor, sequence of RNA on tRNA molecules. Further RNase P is one of two known multiple turnover ribozymes in nature (the other being the ribosome).
- RNase H is a ribonuclease that cleaves the RNA in a DNA/RNA duplex to produce. 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. In contrast to other ribonucleases, such as RNase A or RNase T1, RNase H leaves a 3'-phosphorylated product.he:רנ"אז