Wu, Q orcid.org/0000-0002-6948-7043 (2019) Structural mechanism of DNA-end synapsis in the non-homologous end joining pathway for repairing double-strand breaks: bridge over troubled ends. Biochemical Society Transactions, 47 (6). pp. 1609-1619. ISSN 0300-5127
Abstract
Non-homologous end joining (NHEJ) is a major repair pathway for DNA double-strand breaks (DSBs), which is the most toxic DNA damage in cells. Unrepaired DSBs can cause genome instability, tumorigenesis or cell death. DNA end synapsis is the first and probably the most important step of the NHEJ pathway, aiming to bring two broken DNA ends close together and provide structural stability for end processing and ligation. This process is mediated through a group of NHEJ proteins forming higher-order complexes, to recognise and bridge two DNA ends. Spatial and temporal understanding of the structural mechanism of DNA-end synapsis has been largely advanced through recent structural and single-molecule studies of NHEJ proteins. This review focuses on core NHEJ proteins that mediate DNA end synapsis through their unique structures and interaction properties, as well as how they play roles as anchor and linker proteins during the process of ‘bridge over troubled ends'.
Metadata
Item Type: | Article |
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Authors/Creators: | |
Copyright, Publisher and Additional Information: | © 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society. This is an author produced version of a paper published in Biochemical Society Transactions. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | DNA damage, DNA repair, DNA-end synapsis, double-strand breaks, non-homologous end joining, single-molecule methods |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 02 Jan 2020 10:57 |
Last Modified: | 12 Dec 2020 01:38 |
Status: | Published |
Publisher: | Portland Press |
Identification Number: | 10.1042/bst20180518 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:154931 |