1                                              Pol mu and Pol lambda thus provide distinct solutions to

2                                              Pol mu bypassed CP and OX adducts with an efficiency of

3                                              Pol mu gene expression did not seem to correlate with th

4 s of the primer, displayed by Pol lambda and Pol mu, are shared by the PolDom of bacterial LigD.

5 hough structurally unrelated, Pol lambda and Pol mu, the two eukaryotic DNA polymerases involved in N

6 th the hypothesis that rNTP incorporation by Pol mu is advantageous in gap-filling synthesis during D

7 urther upstream of this position; this makes Pol mu more flexible but also less accurate than Pol lam

8 vely, the Family X member DNA polymerase mu (Pol mu) incorporates rNTPs almost as efficiently as deox

9 ncorporation kinetics by wildtype and mutant Pol mu indicates that rNTP accommodation involves synerg

10 ures of pre- and post-catalytic complexes of Pol mu with a ribonucleotide bound at the active site.

11  beta is at least 4-fold higher than that of Pol mu and approximately 2-fold higher than that of Pol

12 ymatic components consisting of polymerases (Pol mu and Pol lambda), a nuclease (the Artemis.DNA-PKcs

13                 These structures reveal that Pol mu binds and incorporates a rNTP with normal active

14 ucleotide is also selected differently, with Pol mu using the unpaired base adjacent to the downstrea