Grundy, Gabrielle J, Moulding, Hayley A, Caldecott, Keith W and Rulten, Stuart L (2014) One ring to bring them all--the role of Ku in mammalian non-homologous end joining. DNA repair, 17. pp. 30-38. ISSN 1568-7856
Full text not available from this repository.Abstract
The repair of DNA double strand breaks is essential for cell survival and several conserved pathways have evolved to ensure their rapid and efficient repair. The non-homologous end joining pathway is initiated when Ku binds to the DNA break site. Ku is an abundant nuclear heterodimer of Ku70 and Ku80 with a toroidal structure that allows the protein to slide over the broken DNA end and bind with high affinity. Once locked into placed, Ku acts as a tool-belt to recruit multiple interacting proteins, forming one or more non-homologous end joining complexes that act in a regulated manner to ensure efficient repair of DNA ends. Here we review the structure and functions of Ku and the proteins with which it interacts during non-homologous end joining.
Item Type: | Article |
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Schools and Departments: | School of Life Sciences > Sussex Centre for Genome Damage and Stability |
Subjects: | Q Science > QP Physiology |
Depositing User: | Stuart Rulten |
Date Deposited: | 18 Sep 2015 12:07 |
Last Modified: | 05 Aug 2016 06:50 |
URI: | http://srodev.sussex.ac.uk/id/eprint/56818 |