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Abstract
Nonhomologous end joining (NHEJ) is a critical DNA double-strand break (DSB) repair pathway required to maintain genome stability. Many prokaryotes possess a minimalist NHEJ apparatus required to repair DSBs during stationary phase, composed of two conserved core proteins, Ku and ligase D (LigD). The crystal structure of Mycobacterium tuberculosis polymerase domain of LigD mediating the synapsis of two noncomplementary DNA ends revealed a variety of interactions, including microhomology base pairing, mismatched and flipped-out bases, and 3' termini forming hairpin-like ends. Biochemical and biophysical studies confirmed that polymerase-induced end synapsis also occurs in solution. We propose that this DNA synaptic structure reflects an intermediate bridging stage of the NHEJ process, before end processing and ligation, with both the polymerase and the DNA sequence playing pivotal roles in determining the sequential order of synapsis and remodeling before end joining.
Original language | English |
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Pages (from-to) | 456-459 |
Number of pages | 4 |
Journal | Science |
Volume | 318 |
DOIs | |
Publication status | Published - 19 Oct 2007 |
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Dive into the research topics of 'Structure of a NHEJ Polymerase-Mediated DNA Synaptic Complex'. Together they form a unique fingerprint.Projects
- 1 Finished
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Fellowship: Dr T Dafforn: Understanding the Role of the Fibrosis Associated Chaperone Hsp47 in Collagen Synthesis
15/12/03 → 31/12/06
Project: Research Councils