Recognition of template-primer and gapped DNA substrates by the human DNA polymerase beta

Journal of Molecular Biology
S RajendranW Bujalowski

Abstract

Interactions between human DNA polymerase beta and the template-primer, as well as gapped DNA substrates, have been studied using quantitative fluorescence titration and analytical ultracentrifugation techniques. In solution, human pol beta binds template-primer DNA substrates with a stoichiometry much higher than predicted on the basis of the crystallographic structure of the polymerase-DNA complex. The obtained stoichiometries can be understood in the context of the polymerase affinity for the dsDNA and the two ssDNA binding modes, the (pol beta)(16) and (pol beta)(5) binding modes, which differ by the number of nucleotide residues occluded by the protein in the complex. The analysis of polymerase binding to different template-primer substrates has been performed using the statistical thermodynamic model which accounts for the existence of different ssDNA binding modes and has allowed us to extract intrinsic spectroscopic and binding parameters. The data reveal that the small 8 kDa domain of the enzyme can engage the dsDNA in interactions, downstream from the primer, in both (pol beta)(16) and (pol beta)(5) binding modes. The affinity, as well as the stoichiometry of human pol beta binding to the gapped DNAs is not affected b...Continue Reading

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Citations

Oct 7, 2014·Journal of Molecular Structure·Wlodzimierz Bujalowski, Maria J Jezewska
Apr 9, 2008·Journal of Cellular Physiology·Kuo-Hsiang Tang, Ming-Daw Tsai
Nov 5, 2014·Biomolecular Concepts·Koan Briggs, Christopher J Fischer
Mar 26, 2002·The Journal of Biological Chemistry·Maria J JezewskaWlodzimierz Bujalowski
Nov 10, 2004·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Leon P OehlersRonald B Walter
Feb 13, 2003·Biochemistry·Jody M HavenerStephen G Chaney

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