Abstract
DNA ligation is an essential step to complete DNA repair, replication and recombination processes. The human genome encodes two divergent, yet structurally similar DNA ligases, LIG1 and LIG3. Each enzyme has unique amino and carboxy‐terminal extensions and the conserved catalytic core is only 22% identical. LIG3 is essential for mitochondrial genome maintenance, but is also expressed ubiquitously as a nuclear isoform. To understand the mechanism and fidelity of human DNA ligation we are working to characterize DNA LIG1 and LIG3 and their associated protein complexes. Transient and steady state kinetic approaches are used to elucidate distinct enzyme conformational changes and the role of the essential metal ions in substrate selection and catalysis. By determining the similarities and differences between these DNA ligase isoforms, we provide new insights into the clinical situations in which mutation or changes in gene expression are associated with diseases such as cancer and primary immune deficiency.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
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