1. DNA polymerase mu: An inflexible scaffold for substrate flexibility
- Author
-
Lars C. Pedersen, Katarzyna Bebenek, Andrea M. Kaminski, and Thomas A. Kunkel
- Subjects
DNA End-Joining Repair ,DNA polymerase ,DNA-Directed DNA Polymerase ,Biochemistry ,Article ,03 medical and health sciences ,chemistry.chemical_compound ,DNA Ligase ATP ,0302 clinical medicine ,Humans ,DNA Breaks, Double-Stranded ,Molecular Biology ,Polymerase ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,DNA ligase ,biology ,fungi ,Substrate (chemistry) ,Cell Biology ,DNA ,Non-homologous end joining ,chemistry ,030220 oncology & carcinogenesis ,biology.protein ,Biophysics ,DNA polymerase mu ,Recombination - Abstract
DNA polymerase μ is a Family X member that participates in repair of DNA double strand breaks (DSBs) by non-homologous end joining. Its role is to fill short gaps arising as intermediates in the process of V(D)J recombination and during processing of accidental double strand breaks. Pol μ is the only known template-dependent polymerase that can repair non-complementary DSBs with unpaired 3´primer termini. Here we review the unique properties of Pol μ that allow it to productively engage such a highly unstable substrate to generate a nick that can be sealed by DNA Ligase IV.
- Published
- 2020