Crystallization (Comment) | Organism |
---|---|
crystal structure of isoform POLB in complex with nicked DNA that represents the 5'-adenylated deoxyribose phosphate-containing base excision repair intermediate. The 5'-AMP-deoxyribose phosphate group is positioned in the lyase active site | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
K68A | mutation has no significant effect on the removal of 5'-AMP-deoxyribose phosphate | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P06746 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | in addition to removal of 5'-deoxyribose phosphate from base excision repair intermediates, enzyme also removes 5'-adenylated deoxyribose phosphate from base excision repair intermediates after abortive ligation | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DNA polymerase beta | - |
Homo sapiens |
PolB | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | isoform POLB expression rescues methyl methanesulfonate sensitivity in aprataxin (hnt3)- and FEN1 (rad27)-deficient yeast. Model suggests that aprataxin hydrolyzes the 5'-AMP group and allows for renewed attempts at processing of the repair intermediate, and the 5'-deoxyribose phosphate may be channeled into the normal base excision repair pathway for isoform POLB deoxyribose phsosphate removal and gap filling. In long-path base excision repair, the blocking intermediates can be processed via flap excision by FEN1. In an alternative mechanism, POLB could play a part by direct removal of the entire 5'-AMP-deoxyribose phosphate blocking group via its deoxyribose phosphate lyase activity | Homo sapiens |