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A DNase footprinting assay [1] is a DNA footprinting technique used in molecular biology/biochemistry that detects DNA-protein interaction by leveraging the fact that a protein bound to DNA often protects it from enzymatic cleavage. This makes it possible to locate a protein binding site on a particular DNA molecule.
DNase I Structure: DNase I is a glycoprotein with a molecular weight of 30,000 Da and a carbohydrate chain of 8-10 residues attached to Asn18 (orange). [3] It is an 𝛼,𝛽-protein with two 6-stranded 𝛽-pleated sheets which form the core of the structure. [4] These two core sheets run parallel, and all others run antiparallel.
In molecular biology, endonucleases are enzymes that cleave the phosphodiester bond within a polynucleotide chain (namely DNA or RNA).Some, such as deoxyribonuclease I, cut DNA relatively nonspecifically (with regard to sequence), while many, typically called restriction endonucleases or restriction enzymes, cleave only at very specific nucleotide sequences.
An electrophoretic mobility shift assay (EMSA) or mobility shift electrophoresis, also referred as a gel shift assay, gel mobility shift assay, band shift assay, or gel retardation assay, is a common affinity electrophoresis technique used to study protein–DNA or protein–RNA interactions. This procedure can determine if a protein or mixture ...
Deoxyribonuclease I (usually called DNase I), is an endonuclease of the DNase family coded by the human gene DNASE1. [5] DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides.
In genetics, DNase I hypersensitive sites (DHSs) are regions of chromatin that are sensitive to cleavage by the DNase I enzyme. In these specific regions of the genome, chromatin has lost its condensed structure, exposing the DNA and making it accessible. This raises the availability of DNA to degradation by enzymes, such as DNase I.
Deoxyribonuclease II (EC 3.1.22.1, DNase II, pancreatic DNase II, deoxyribonucleate 3'-nucleotidohydrolase, pancreatic DNase II, acid deoxyribonuclease, acid DNase) is an endonuclease that hydrolyzes phosphodiester linkages of deoxyribonucleotide in native and denatured DNA, yielding products with 3'-phosphates and 5'-hydroxyl ends, which occurs as a result of single-strand cleaving mechanism. [1]
Of particular interest are DNA ligases. [6] These molecules have demonstrated remarkable chemoselectivity in RNA branching reactions. Although each repeating unit in a RNA strand owns a free hydroxyl group, the DNA ligase takes just one of them as a branching starting point.