Escherichia coli uvrD mutants with thermosensitive DNA-dependent adenosine triphosphatase I (helicase II).
Three mutants producing thermosensitive DNA-dependent Adenosine triphosphatase (ATPase) I were screened from a collection of temperature-sensitive mutants of Escherichia coli K12. ATPase I purified to near homogeneity from one of the mutants (JE11000) possesses both thermosensitive DNA-dependent ATPase and DNA helicase activities. We have shown that ATPase I is encoded by the uvrD gene as first suggested by Oeda et al. (1982): (i) the thermosensitive ATPase I mutation present in JE11040 lies in or very close to the uvrD gene, (ii) ATPase I activity is absent in uvrD210, uvrD156, and uvrD252 mutants. Thus the thermosensitive mutations correspond to new uvrD mutations. However, the mutation present in JE11040 confers neither UV sensitivity nor mutator phenotype at high temperature. Evidence is presented that the mutant ATPase I is stabilized in vivo at 42 degrees C.
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D004265:DNA Helicases; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D009154:Mutation; D013696:Temperature; D014466:Ultraviolet Rays
D029968:Escherichia coli Proteins; D000251:Adenosine Triphosphatases; C506746:UvrD protein, E coli; D004265:DNA Helicases