Table 1.
Spontaneous mutation rates in strains with dpb3Δ and dpb4Δ, pol2-4 mutation, msh6Δ, and pol-5DV.
Table 2.
Mutations generated by exonuclease-deficient Pol ε in vitro.
Table 3.
Influence of rev3Δ on spontaneous mutagenesis in the strain lacking DPB3 and DPB4 genes.
Table 4.
Spontaneous mutation rates in strains with dpb3Δ dpb4Δ and mismatch repair deficiency.
Table 5.
CAN1 forward mutation spectrum.
Figure 1.
Processivity of the polymerase activity of Pol ε holoenzyme and Pol2/Dpb2 complex.
(A) A 50 nt long, 32P-5′end-labeled, oligonucleotide was annealed to pBluescript II SK (+) ssDNA and used as a DNA substrate in the polymerization assay. (B) Shown is the image of extension products generated by four-subunit Pol ε and a two-subunit Pol2/Dpb2 complex, separated on a 8% denaturing polyacrylamide gel (for details see Materials and Methods). A DNA sequencing ladder with the identical template was used as a molecular weight marker on the right hand. Reaction times are indicated under each lane. (C) The termination probability at each position on the template was calculated for the four-subunit Pol ε holoenzyme and Pol2/Dpb2 complex (for details see Materials and Methods).
Figure 2.
Processivity of the exonuclease activity of Pol ε holoenzyme and Pol2/Dpb2 complex.
(A) A 57 nt long, 32P-5′end-labeled, oligonucleotide was annealed to a 75 nt oligonucleotide, creating a primer-template to be used as a DNA substrate in the exonuclease assay. (B) Shown is the image of degradation products generated by four-subunit Pol ε and two-subunit Pol2/Dpb2 complex, separated on a 12% denaturing polyacrylamide gel (for details see Materials and Methods). Reaction times are indicated above each lane. (C) The termination probability at each position on the template was calculated for the four-subunit Pol ε holoenzyme and Pol2/Dpb2 complex (for details see Materials and Methods).