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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.
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.
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.
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 ...
The restriction endonuclease Fok1, naturally found in Flavobacterium okeanokoites, is a bacterial type IIS restriction endonuclease consisting of an N-terminal DNA-binding domain and a non sequence-specific DNA cleavage domain at the C-terminal. [2]
The genomic DNA for ERCC1 was the first human DNA repair gene to be isolated by molecular cloning. The original method was by transfer of fragments of the human genome to ultraviolet light (UV)-sensitive mutant cell lines derived from Chinese hamster ovary cells. [9]
Non-specific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. Mismatch binding induces ATP uptake and a conformational change in the MutS protein, resulting in a clamp that translocates on DNA. MutS is a modular protein with a complex structure, [5] and is composed of:
It was cloned in 1987 and shown to consist of a 266 protein precursor, [6] which is further cleaved and secreted as a 245 amino acid active nuclease. [7] Its active form in solution is a homodimer. [8] It has two disulfide bonds, the first between cysteine 30 & 34 and the second between cysteine 222 & 264. [7]