Open AccessEffect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease.
Author(s) -
Intisar Husain,
Bennett Van Houten,
David C. Thomas,
Mahmoud M. Abdel-Monem,
Aziz Sancar
Publication year - 1985
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.20.6774
Subject(s) - nucleotide excision repair , helicase , nuclease , dna polymerase , microbiology and biotechnology , dna polymerase ii , dna clamp , dna , dna repair , dna polymerase i , biology , replication protein a , oligonucleotide , polymerase , chemistry , biochemistry , dna binding protein , polymerase chain reaction , gene , reverse transcriptase , rna , transcription factor
UvrABC excision nuclease (UvrA, UvrB, and UvrC proteins) of Escherichia coli removes nucleotide mono- and diadducts from DNA in the form of oligonucleotides 12 or 13 bases long. We find that the purified enzyme dissociates from DNA very slowly, if at all, in the absence of other proteins implicated in excision repair. Addition of DNA polymerase I and helicase II (UvrD protein) to the reaction mixture stimulates the turnover rate of the excision nuclease to a level comparable to that observed in vivo.