endonuclease

restriction enzyme

Protein (more specifically, an endonuclease) produced by bacteria that cleaves DNA at specific sites along its length. Thousands have been found, from many different bacteria; each recognizes a specific nucleotide sequence. In the living bacterial cell, these enzymes destroy the DNA of certain invading viruses (bacteriophages), thus placing a “restriction” on the number of viral strains that can cause infection; the bacterium's own DNA is protected from cleavage by methyl (singlehorzbondCH3) groups, which are added by enzymes at the recognition sites to mask them. In the laboratory, restriction enzymes allow researchers to isolate DNA fragments of interest, such as those that contain genes, and to recombine them with other DNA molecules; for this reason they have become very powerful tools of recombinant DNA biotechnology (see DNA recombination).

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Endonucleases are enzymes that cleave the phosphodiester bond within a polynucleotide chain, in contrast to exonucleases, which cleave phosphodiester bonds at the end of a polynucleotide chain. Restriction endonucleases (Restriction Enzymes) cleave DNA at specific sites, and are divided into three categories, Type I, Type II, and Type III, according to their mechanism of action. These enzymes are often used in genetic engineering to make recombinant DNA for introduction into bacterial, plant, or animal cells.

Common endonucleases:

Restriction endonucleases (ENases) are products of bacteria, and can be used to map a piece of DNA.

Bacterial:

  1. UvrABC endonuclease is a well documented endonuclease found in E.coli.

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