Holliday junction-resolving enzymes - structures and mechanisms

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

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    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


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