Understanding T7 Endonuclease I in 60 Seconds

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T7 Endonuclease I is a dimeric nuclease that plays a crucial role in DNA repair and is widely utilized in molecular biology research. This enzyme is highly selective for four-way DNA junctions, also known as Holliday junctions. Its structure as a dimer, with a flexible N-terminal region, is essential for its function. T7 Endonuclease I binds to DNA junctions and cleaves them, with the N-terminus being crucial for generating a local opening at the center of the DNA junction, enabling efficient cleavage. The enzyme has gained significant importance in genome editing applications, where it is used to detect and quantify targeted mutations. Its ability to recognize and cleave mismatches and extrahelical loops in double-stranded DNA makes it valuable for assessing the efficiency of genome targeting techniques like CRISPR, TALENs, and ZFNs. Additionally, T7 Endonuclease I has shown effectiveness in removing mutations that accumulate during artificial gene synthesis, thereby improving the fidelity of synthesized genes. The enzyme is routinely employed in mismatch cleavage assays to detect the presence of indels resulting from genome editing experiments. When used in genome editing validation, T7 Endonuclease I recognizes and cleaves heteroduplex DNA formed by the annealing of wild-type and mutant DNA strands, allowing researchers to estimate the efficiency of genome targeting. Its versatility and specific DNA structure recognition capabilities make T7 Endonuclease I an indispensable tool in various aspects of molecular biology research.

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