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In molecular biology, enzymes in the DNA/RNA non-specific endonuclease family of bacterial and eukaryotic endonucleases EC 3.1.30.-share the following characteristics: they act on both DNA and RNA, cleave double-stranded and single-stranded nucleic acids and require a divalent ion such as magnesium for their activity.
Evidence suggests that endonuclease activity experiences a lag compared to exonuclease activity. [2] Restriction enzymes are endonucleases from eubacteria and archaea that recognize a specific DNA sequence. [3] The nucleotide sequence recognized for cleavage by a restriction enzyme is called the restriction site.
The non-specific DNA cleavage domain from the end of the FokI endonuclease can be used to construct hybrid nucleases that are active in a yeast assay. [6] [7] These reagents are also active in plant cells [8] [9] and in animal cells.
It is a representative of the DNA/RNA non-specific endonuclease family. ... (A current notable non-producer is New England Biolabs) [23] See also
RNase H is a non-specific endonuclease and catalyzes the cleavage of RNA via a hydrolytic mechanism, aided by an enzyme-bound divalent metal ion. RNase H leaves a 5'-phosphorylated product. [7] EC 3.1.26.3: RNase III is a type of ribonuclease that cleaves rRNA (16s rRNA and 23s rRNA) from transcribed polycistronic RNA operon in prokaryotes. It ...
MutH recognizes hemimethylated 5'—GATC—3' sites and cleaves next to the G of the non-methylated strand (the more recently synthesized strand). VSP repair is initiated by the endonuclease Vsr. It corrects a specific T/G mismatch caused by the spontaneous deamination of methylated cytosines to thymines.
Nuclease S1 (EC 3.1.30.1) is an endonuclease enzyme that splits single-stranded DNA (ssDNA) and RNA into oligo- or mononucleotides. This enzyme catalyses the following chemical reaction. Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
The non-specific cleavage domain from the type IIs restriction endonuclease FokI is typically used as the cleavage domain in ZFNs. [4] This cleavage domain must dimerize in order to cleave DNA [5] and thus a pair of ZFNs are required to target non-palindromic DNA sites. Standard ZFNs fuse the cleavage domain to the C-terminus of each zinc ...