2006
DOI: 10.1074/jbc.m601178200
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Up-regulation of the Fidelity of Human DNA Polymerase λ by Its Non-enzymatic Proline-rich Domain

Abstract: DNA repair pathways are essential for maintaining genome stability. DNA polymerase ␤ plays a critical role in base-excision repair in vivo. DNA polymerase , a recently identified X-family homolog of DNA polymerase ␤, is hypothesized to be a second polymerase involved in base-excision repair. The full-length DNA polymerase is comprised of three domains: a C-terminal DNA polymerase ␤-like domain, an N-terminal BRCA1 C-terminal domain, and a previously uncharacterized proline-rich domain. Strikingly, pre-steady-s… Show more

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Cited by 41 publications
(75 citation statements)
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“…For Pols ␤ and , the K d was weakened by 5-fold on average and the k p was reduced by 11-fold on average compared to dATP. Notably, Pols ␤ and have different kinetic parameters, which supports our previous discovery that these two homologs of the X-family possess different enzymatic properties (1,15). In contrast, Pol maintained a tight enzyme-DNA-PMPA-DP complex, but the rate of PMPA-DP incorporation opposite template dT dropped by 2,600-fold.…”
Section: Resultssupporting
confidence: 78%
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“…For Pols ␤ and , the K d was weakened by 5-fold on average and the k p was reduced by 11-fold on average compared to dATP. Notably, Pols ␤ and have different kinetic parameters, which supports our previous discovery that these two homologs of the X-family possess different enzymatic properties (1,15). In contrast, Pol maintained a tight enzyme-DNA-PMPA-DP complex, but the rate of PMPA-DP incorporation opposite template dT dropped by 2,600-fold.…”
Section: Resultssupporting
confidence: 78%
“…The plasmids, expression, and purification of human DNA polymerases ␤ (5, 39), (15), (48), truncated (residues 1 to 420) (48), truncated (residues 9 to 518) (48), and truncated Rev1 (residues 341 to 829) (32, 33) were described previously. Commercially synthesized oligomers listed in Table 1 were purified using polyacrylamide gel electrophoresis (14,16 2 , 100 mM NaCl, 0.1 mM EDTA, 5 mM DTT, 10% glycerol, and 0.1 mg/ml of BSA) for Pol (14,15), and buffer Y (50 mM HEPES [pH 7.5] at 37°C with 5 mM MgCl 2 , 50 mM NaCl, 0.1 mM EDTA, 5 mM DTT, 10% glycerol, and 0.1 mg/ml of BSA) for Pols , , , and Rev1. Pols , , , and Rev1 were assayed with the 21-41-mer DNA substrates, and Pols ␤ and were assayed with the 21-19-41-mer single-nucleotide-gap DNA substrates.…”
Section: Methodsmentioning
confidence: 99%
“…Thus, we confirmed the PCNA dependency of pol δ on a different primer/template containing all four nucleotides (Fig. S1C: compare lanes 2-8 to lanes [9][10][11][12][13][14][15]. A distinct pausing of pol δ at the nucleotide preceeding 8-oxo-G was observed, as indicated by an accumulation of a prominent band (Fig.…”
Section: Resultssupporting
confidence: 66%
“…Importantly, however, this occurred only with C and not with A and depended on the amounts of pol λ in the reactions ( Fig. 2A: compare lanes 6-10 to lanes [11][12][13][14][15]. Also, the FL product generated by pol δ increased as a function of pol λ, but only in the presence of C ( Fig.…”
Section: Resultsmentioning
confidence: 99%
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