Journal article
Yeast DNA Polymerase η Utilizes an Induced-Fit Mechanism of Nucleotide Incorporation
Cell (Cambridge), Vol.107(7), pp.917-927
12/28/2001
DOI: 10.1016/S0092-8674(01)00613-4
PMID: 11779467
Abstract
DNA polymerase eta (Poleta) is unique among eukaryotic DNA polymerases in its proficient ability to replicate through distorting DNA lesions, and Poleta synthesizes DNA with a low fidelity. Here, we use pre-steady-state kinetics to investigate the mechanism of nucleotide incorporation by Poleta and show that it utilizes an induced-fit mechanism to selectively incorporate the correct nucleotide. Poleta discriminates poorly between the correct and incorrect nucleotide at both the initial nucleotide binding step and at the subsequent induced-fit conformational change step, which precedes the chemical step of phosphodiester bond formation. This property enables Poleta to bypass lesions with distorted DNA geometries, and it bestows upon the enzyme a low fidelity.
Details
- Title: Subtitle
- Yeast DNA Polymerase η Utilizes an Induced-Fit Mechanism of Nucleotide Incorporation
- Creators
- M Todd Washington - Sealy Center for Molecular Science, University of Texas Medical Branch at Galveston, 6.104 Blocker Medical Research Building, 11th and Mechanic Streets, Galveston, TX 77555, USALouise PrakashSatya Prakash
- Resource Type
- Journal article
- Publication Details
- Cell (Cambridge), Vol.107(7), pp.917-927
- Publisher
- United States
- DOI
- 10.1016/S0092-8674(01)00613-4
- PMID
- 11779467
- ISSN
- 0092-8674
- eISSN
- 1097-4172
- Grant note
- GM 19261 / NIGMS NIH HHS
- Language
- English
- Date published
- 12/28/2001
- Academic Unit
- Radiation Oncology; Biochemistry and Molecular Biology
- Record Identifier
- 9984025272502771
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