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Literature summary for 4.2.99.B1 extracted from

  • Caglayan, M.; Batra, V.K.; Sassa, A.; Prasad, R.; Wilson, S.H.
    Role of polymerase beta in complementing aprataxin deficiency during abasic-site base excision repair (2014), Nat. Struct. Mol. Biol., 21, 497-499.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Protein Variants Comment Organism
K68A mutation has no significant effect on the removal of 5'-AMP-deoxyribose phosphate Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P06746
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-

Substrates and Products (Substrate)

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 ?
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?

Synonyms

Synonyms Comment Organism
DNA polymerase beta
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Homo sapiens
PolB
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Homo sapiens

General Information

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