Evidence implying DNA polymerase β function in excision repair

• Published in: Nucleic acids research 1980-01, Vol.8 (2), p.361-375
• Main Authors: Siedlecki, J.A., Szyszko, J., Pietrzykowska, I., Zmudzka, B.
• Format: Article
• Language: English
• Subjects: Animals; Cattle; Deoxyribonuclease I; Deoxyribonucleases - metabolism; DNA Nucleotidyltransferases - metabolism; DNA Polymerase I - metabolism; DNA Polymerase II - metabolism; DNA Repair; DNA Replication; DNA-Directed DNA Polymerase - metabolism; Endonucleases - metabolism; Escherichia coli; Kinetics; Templates, Genetic; Thymus Gland - enzymology
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/8.2.361

Comparison was made of the ability of calf thymus DNA polymerases α and β to replicate the following templates: native E. coli CR-34 DNA (T-DNA), calf thymus DNA activated by DNase I (act .DNA), BU-DHA (from E. coli CR-34 cells cultured on BUdR-containing medium) with damages resulting from incomplete excision repair, as well as thermally denatured act.DNA and BU-DNA (s.s.act.DNA and s.s.BU-DNA). 3H-TTP Incorparation during extensive replication of act.DNA was similar far both enzymes, being, as expected, 40 times higher than far T-DNA. Likewise, the differences in the yield of the s.s.act.DNA or s.S.BU-DNA replication between both enzymes were negligible. In contrast, damaged native DNA was 6–30 times more extensively replicated by DNA polymerase β than α. We propose that this is due to the greater ability of DNA polymerase β compared with α to replicate single-stranded gaps, the presence of which is more likely in damaged BU-DNA than in T-DNA and act.DNA.