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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.
The ERCC1–XPF complex is a structure-specific endonuclease. ERCC1-XPF does not cut DNA that is exclusively single-stranded or double-stranded, but it cleaves the DNA phosphodiester backbone specifically at junctions between double-stranded and single-stranded DNA.
The protein forms a heterodimer with MLH1 and this complex interacts with MSH2 bound to mismatched bases. Defects in this gene are associated with hereditary nonpolyposis colorectal cancer, with Turcot syndrome, and are a cause of supratentorial primitive neuroectodermal tumors. Alternatively spliced transcript variants have been observed.
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]
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 ...
Therefore, bifunctional glycosylases can convert a base lesion into a single-strand break without the need for an AP endonuclease. β-Elimination of an AP site by a glycosylase-lyase yields a 3' α,β-unsaturated aldehyde adjacent to a 5' phosphate, which differs from the AP endonuclease cleavage product. [5]