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Literature summary for 6.5.1.1 extracted from
- ATP-type DNA ligase requires other proteins for its activity in vitro and its operon components for radiation resistance in Deinococcus radiodurans in vivo (2010), Biochem. Cell Biol., 88, 783-790.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| DRB0098 protein | DNA ligase activity of LigB is severalfold stimulated by PprA in the presence of the recombinant DRB0098 protein | Deinococcus radiodurans | |
| PprA protein | DNA ligase activity of LigB is severalfold stimulated by PprA in the presence of the recombinant DRB0098 protein | Deinococcus radiodurans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Deinococcus radiodurans | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP-type DNA repair ligase | - |
Deinococcus radiodurans |
| drB0100 | - |
Deinococcus radiodurans |
| LigB | - |
Deinococcus radiodurans |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | a drB0100 gene deletion mutant exhibits a nearly 2-log cycle reduction in growth rate when exposed to a 10000 Gray dose of gamma-radiation and a significant loss in mitomycin C and methylmethane sulfonate tolerance as compared to the wild type | Deinococcus radiodurans |
| physiological function | the LigB operon components contribute to radiation resistance and double-strand break repair in Deinococcus radiodurans | Deinococcus radiodurans |
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