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Additional recommended knowledge
The preferred substrates are blunt or recessed 3´-termini, although ExoIII also acts at nicks in duplex DNA to produce single-strand gaps. The enzyme is not active on single-stranded DNA, and thus 3´-protruding termini are resistant to cleavage. The degree of resistance depends on the length of the extension, with extensions 4 bases or longer being essentially resistant to cleavage. This property is used to produce unidirectional deletions from a linear molecule with one resistant (3´-overhang) and one susceptible (blunt or 5´-overhang) terminus .
ExoIII activity depends partially on the DNA helical structure  and displays sequence dependence (C>A=T>G) .
ExoIII has also been reported to have RNase H, 3´-phosphatase and AP-endonuclease activities .
Temperature, salt concentration and the ratio of enzyme to DNA greatly affect enzyme activity, requiring reaction conditions to be tailored to specific applications.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Exonuclease_III". A list of authors is available in Wikipedia.|