Structure and Mechanism of DNA Polymerase β
Year: 2014
Type: article
Abstract: DNA polymerase (pol) β is a small eukaryotic DNA polymerase composed of two domains. Each domain contributes an enzymatic activity (DNA synthesis and deoxyribose phosphate lyase) during the repair of simple base lesions. These domains are termed the polymerase and lyase domains, respectively. Pol β has been an excellent model enzyme for studying the nucleotidyl transferase reaction and substrate discrimination at a molecular level. In this review, recent crystallographic studies of pol β in various liganded and conformational states during the insertion of right and wrong nucleotides as well as during the bypass of damaged DNA (apurinic sites and 8-oxoguanine) are described. Structures of these catalytic intermediates provide unexpected insights into mechanisms by which DNA polymerases enhance genome stability. These structures also provide an improved framework that permits computational studies to facilitate the interpretation of detailed kinetic analyses of this model enzyme.
Source: Biochemistry
DOI: 10.1021/bi500139h
Authors: William A. Beard, Samuel H. Wilson
Language: English
Topic: DNA Repair Mechanisms
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $4,500
Awards: Mechanisms of Nucleic Acid Enzymes - Pol Beta and Mammalian Base Repair Enzymes, Biology of Mammalian Base Excision Repair, Resource for Biocomputing, Visualization, and Informatics, DNA Polymerase Fidelity Mechanisms: Theory and Experiment, G8491381323, DNA Polymerase Fidelity Mechanisms: Theory and Experiment, G9000281357
OpenAlex ID: W3121702821