Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of PolB-knockout mouse embryonic fibroblasts (MEFs)Mbeta19tsA, phenotype. Mouse embryonic fibroblasts (MEFs) deficient in enzyme PolB show significantly increased sensitivity to methyl methanesulfonate (MMS). Wild-type MEFs and PolB-knockout MEFs are transfected with shRNA-expression vectors for Apex knockdown. Apex knockdown has essentially no effect on cell viability in the presence or absence of PolB. Thus, Apex knockdown does not affect the number of viable cells immediately after MMS treatment. The MMS sensitivity depends on Apex protein levels and suggest that resistance at low concentrations of MMS is due to an Apex-dependent/PolB-independent repair mechanism | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P06746 | - |
- |
Mus musculus | Q8K409 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryonic fibroblast | MEFs | Mus musculus | - |
Mbeta16tsA cell | - |
Mus musculus | - |
Synonyms | Comment | Organism |
---|---|---|
DNA polymerase beta | - |
Homo sapiens |
DNA polymerase beta | - |
Mus musculus |
pol beta | - |
Homo sapiens |
pol beta | - |
Mus musculus |
PolB | - |
Homo sapiens |
PolB | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
assay at | Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | mouse embryonic fibroblasts (MEFs) deficient in enzyme PolB show significantly increased sensitivity to methyl methanesulfonate (MMS). PolB deficiency results in an increased apoptotic cell fraction and chromosomal aberrations after MMS treatment. MMS hypersensitivity can be reversed by the dRP lyase domain of PolB, this hypersensitivity is mainly caused by Sn-BER deficiency. A contribution of PolB-independent repair mechanisms is also likely because of the increased sensitivity of PolB-knockout MEFs at relatively high MMS concentrations | Mus musculus |
metabolism | because DNA polymerase lambda (PolL) belongs to the same family X and has similarities in activity and structure to PolB, PolL may play a backup role in the absence of PolB | Mus musculus |
physiological function | DNA polymerase beta (PolB) has both DNA polymerase and dRP lyase activities. Enzyme PolB plays a dominant role in single nucleotide (Sn-) BER by incorporating a nucleotide and removing 5'-dRp. Methyl methanesulfonate (MMS)-induced damage is repaired by Sn-BER | Homo sapiens |
physiological function | DNA polymerase beta (PolB) has both DNA polymerase and dRP lyase activities. Enzyme PolB plays a dominant role in single nucleotide (Sn-) BER by incorporating a nucleotide and removing 5'-dRp. Methyl methanesulfonate (MMS)-induced damage is repaired by Sn-BER. Resistance at low concentrations of MMS is due to an Apex-dependent/PolB-independent repair mechanism | Mus musculus |