Projects per year
Abstract
Holliday junction-resolving enzymes are nucleases that are highly specific for the structure of the junction, to which they bind in dimeric form. Two symmetrically-disposed cleavages are made. These are not simultaneous, but the second cleavage is accelerated relative to the first, so ensuring that bilateral cleavage occurs during the lifetime of the DNA-protein complex. In eukaryotic cells there are two known junction-resolving activities. GEN1 is similar to enzymes from lower organisms. A crystallographic structure of a fungal GEN1 bound to the product of resolution has been determined. These complexes are dimerized within the crystal lattice such that the strands of the products may be simply reconnected to form a junction. These structures suggest a trajectory for the resolution process. This article is protected by copyright. All rights reserved.
Original language | English |
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Pages (from-to) | 1073-1082 |
Number of pages | 10 |
Journal | FEBS Letters |
Volume | 591 |
Issue number | 8 |
Early online date | 19 Dec 2016 |
DOIs | |
Publication status | Published - Apr 2017 |
Keywords
- Genetic recombination
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Dive into the research topics of 'Holliday junction-resolving enzymes - structures and mechanisms'. Together they form a unique fingerprint.Projects
- 2 Finished
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Dynamics of Eukaryotic Junction-Resolving Enzyme GEN1 - DNA Junction Interactions
Lilley, D. (Investigator)
Biotechnology and Biological Sciences Research Council
1/10/16 → 30/09/19
Project: Research
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Fluorescence Resonance Energy Transfer as a Rich Source of Orientational Information in Nucleic Acid Structure
Lilley, D. (Investigator)
Engineering and Physical Sciences Research Council
1/09/12 → 30/06/16
Project: Research