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Binding and catalysis by OGG1 deletion mutants
figure
posted on 2011-12-30, 17:52 authored by Jeff W. Hill, Michele K. EvansCopyright information:
Taken from "Dimerization and opposite base-dependent catalytic impairment of polymorphic S326C OGG1 glycosylase"
Nucleic Acids Research 2006;34(5):1620-1632.
Published online 20 Mar 2006
PMCID:PMC1405821.
© The Author 2006. Published by Oxford University Press. All rights reserved
() Amino acid sequence of the C-termini of wild-type, wild-type CΔ19, S326C, S326C CΔ19 and CΔ20 OGG1. () Wild-type OGG1 (lane 1) was reacted with an 8-oxoG·C substrate as described in . Identical reactions were carried out for wild-type CΔ19 (lane 2), S326C (lane 3), S326C CΔ19 (lane 4) and CΔ20 OGG1 (lane 5). () Graphical representation of actual data shown in (B). () Binding of OGG1 enzymes to an 8-oxoG·C substate was measured by electrophoretic shift assay as described in . Lane 1, no enzyme; lane 2, wild-type; lane 3 wild-type CΔ19; lane 4, S326C; lane 5, S326C CΔ19; and lane 6 CΔ20 OGG1. () Graphical representation of actual data shown in (D). Inset, dissociation constants calculated from data shown in ().