Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | uracil DNA glycosylase activity on nucleosomal DNA depends on rotational orientation of targets | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | association of linker histone reduces activity of UDG at selected sites near where the globular domain of H1 is proposed to bind to the nucleosome as well as within the extra-core DNA | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P12295 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | preparation of a set of model nucleosome substrates, of 154mer DNA, in which single thymidine residues are replaced with uracil at specific locations and a second set of nucleosomes in which uracils are randomly substituted for all thymidines. UDG efficiently removes uracil from internal locations in the nucleosome where the DNA backbone is oriented away from the surface of the histone octamer, without significant disruption of histone-DNA interactions. However, uracils at sites oriented toward the histone octamer surface are excised at much slower rates, consistent with a mechanism requiring spontaneous DNA unwrapping from the nucleosome. In contrast to the nucleosome core, UDG activity on DNA outside the core DNA region is similar to that of naked DNA, overview | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
UDG | - |
Escherichia coli |
uracil DNA glycosylase | - |
Escherichia coli |