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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 Pol mu tolerates 8OG-containing template DNA substrates,
7 hough structurally unrelated, Pol lambda and Pol mu, the two eukaryotic DNA polymerases involved in N
8 NA polymerase (Pol) X family members such as Pol mu and terminal deoxynucleotidyl transferase (TdT) a
9 th the hypothesis that rNTP incorporation by Pol mu is advantageous in gap-filling synthesis during D
12 urther upstream of this position; this makes Pol mu more flexible but also less accurate than Pol lam
13 junction with a Pol X construct that mimics Pol mu in a reconstituted system explained the distincti
14 DNA polymerases lambda (Pol lambda) and mu (Pol mu), members of the Pol X family, play a key role in
15 '-guanosine (8OG) by Family X Polymerase mu (Pol mu) in steady-state kinetics and cell-based assays.
16 vely, the Family X member DNA polymerase mu (Pol mu) incorporates rNTPs almost as efficiently as deox
17 ncorporation kinetics by wildtype and mutant Pol mu indicates that rNTP accommodation involves synerg
18 ures of pre- and post-catalytic complexes of Pol mu with a ribonucleotide bound at the active site.
19 e, we used a chimeric TdT harboring Loop1 of Pol mu that recapitulated the functional properties of P
22 beta is at least 4-fold higher than that of Pol mu and approximately 2-fold higher than that of Pol
23 ymatic components consisting of polymerases (Pol mu and Pol lambda), a nuclease (the Artemis.DNA-PKcs
25 zation of template 8OG bypass indicates that Pol mu inserts adenosine nucleotides with weak sugar sel
27 that the template 8OG is accommodated in the Pol mu active site with none of the DNA substrate distor
29 ucleotide is also selected differently, with Pol mu using the unpaired base adjacent to the downstrea