Open AccessIsolation and characterization of inhibitory factors of DNA polymerase III holoenzyme from Escherichia coli
Author(s) -
Hase Masakazu,
Mizushima Tohru,
Katayama Tsutomu,
Sekimizu Kazuhisa
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07723.x
Subject(s) - dna polymerase i , klenow fragment , dna clamp , dna polymerase , dna polymerase ii , polymerase , escherichia coli , microbiology and biotechnology , biology , dna , biochemistry , polymerase chain reaction , exonuclease , reverse transcriptase , gene
Abstract We isolated fractions by Mono Q chromatography that inhibited the activity of Escherichia coli DNA polymerase III holoenzyme using an assay system with a primed single‐stranded DNA template coated with single‐stranded DNA binding protein (SSB). The inhibitory activities were inactivated by heat‐treatment at 100 °C for 10 min, suggesting that they are proteins. The factors did not inhibit the activity of RNA polymerase of Escherichia coli . The inhibitory effects were less potent for the activities of the large (Klenow) fragment of DNA polymerase I and T4 DNA polymerase than for DNA polymerase HI holoenzyme. No degradation of single‐or double‐stranded DNA was observed in the fractions, indicating that inhibition was not due to degradation of the DNA.