Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli BL21(DE3) cells | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | Q5ZND2 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DNA + H2O | single-site cleavage is solely a result of the interaction between two independent enzymes: a cis-acting enzyme which is bound to its recognition site in the DNA and a trans-acting enzyme either bound to or activated by its substrate in ATP-dependent manner. The two cooperating enzymes in solution can come together via diffusion. For cleavage to happen, the interaction between the two nucleases should occur within a time period shorter than the time required by the enzyme in cis to leave its recognition site. In case of EcoP15I, this time is measured to be about 6-17 seconds. According to a model of DNA cleavage a recognition site bound Type III RM enzyme would undergo a conformational change induced by the hydrolysis of ATP making it both diffusion-competent and nucleolytically active. The activated nuclease can catalyze single-strand scission only in cooperation with another ATP-activated nuclease. It is proposed that this model is valid for both single-site and two-site cleavage, except that in single-site cleavage the cooperating nucleases come together by 3D diffusion, and in two-site cleavage they converge by 1D diffusion and/or looping | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
EcoP15I | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | Type III RM enzymes are bacterial defense systems that protect the host from invading foreign DNA by nucleolytically cleaving them at specific recognition sites | Escherichia coli |