Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.99.B1 extracted from

  • Yamamoto, R.; Umetsu, M.; Yamamoto, M.; Matsuyama, S.; Takenaka, S.; Ide, H.; Kubo, K.
    AP endonuclease knockdown enhances methyl methanesulfonate hypersensitivity of DNA polymerase beta knockout mouse embryonic fibroblasts (2015), J. Radiat. Res., 56, 462-466 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.99.B1

Protein Variants

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

Organism UniProt Comment Textmining
Homo sapiens P06746
-
-
Mus musculus Q8K409
-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryonic fibroblast MEFs Mus musculus
-
Mbeta16tsA cell
-
 Mus musculus
-

Synonyms

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 assay at Mus musculus

General Information

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