Holliday junction-resolving enzymes - structures and mechanisms

David M. J. Lilley (Lead / Corresponding author)

Research output: Contribution to journalReview articlepeer-review

9 Citations (Scopus)
228 Downloads (Pure)


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 languageEnglish
Pages (from-to)1073-1082
Number of pages10
JournalFEBS Letters
Issue number8
Early online date19 Dec 2016
Publication statusPublished - Apr 2017


  • Genetic recombination


Dive into the research topics of 'Holliday junction-resolving enzymes - structures and mechanisms'. Together they form a unique fingerprint.

Cite this