Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation.

Cell (2001), Volume 107, Page 917

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.

Polymerases:

Topics:

Nucleotide Incorporation, Kinetic Parameters

Status:

new topics/pols set partial results complete validated

Results:

Polymerase Reference Property Result Context
Human Pol eta Washington MT2001 Processivity 0.84bp
Human Pol eta Washington MT2001 Vmax 1.3 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
Human Pol eta Washington MT2001 Kd 2.4nM Reaction: Nucleotide incorporation; Substrate: dATP
Human Pol eta Washington MT2001 Kd 13uM Reaction: Misincorporation; Substrate: dCTP
Human Pol eta Washington MT2001 Kd 11nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol eta Washington MT2001 kcat 0.01 /second Reaction: Nucleotide incorporation; Substrate: dNTPs

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