TY - JOUR
A2 - Basu, Ashis
AU - Brown, Jessica A.
AU - Zhang, Likui
AU - Sherrer, Shanen M.
AU - Taylor, John-Stephen
AU - Burgers, Peter M. J.
AU - Suo, Zucai
PY - 2010
DA - 2010/07/25
TI - Pre-Steady-State Kinetic Analysis of Truncated and Full-Length Saccharomyces cerevisiae DNA Polymerase Eta
SP - 871939
VL - 2010
AB - Understanding polymerase fidelity is an important objective towards ascertaining the overall stability of an organism's genome. Saccharomyces cerevisiae DNA polymerase η (yPolη), a Y-family DNA polymerase, is known to efficiently bypass DNA lesions (e.g., pyrimidine dimers) in vivo. Using pre-steady-state kinetic methods, we examined both full-length and a truncated version of yPolη which contains only the polymerase domain. In the absence of yPolη's C-terminal residues 514–632, the DNA binding affinity was weakened by 2-fold and the base substitution fidelity dropped by 3-fold. Thus, the C-terminus of yPolη may interact with DNA and slightly alter the conformation of the polymerase domain during catalysis. In general, yPolη discriminated between a correct and incorrect nucleotide more during the incorporation step (50-fold on average) than the ground-state binding step (18-fold on average). Blunt-end additions of dATP or pyrene nucleotide 5′-triphosphate revealed the importance of base stacking during the binding of incorrect incoming nucleotides.
SN - 2090-0201
UR - https://doi.org/10.4061/2010/871939
DO - 10.4061/2010/871939
JF - Journal of Nucleic Acids
PB - SAGE-Hindawi Access to Research
KW -
ER -