4.5 Review

Holliday junction-resolving enzymes-structures and mechanisms

期刊

FEBS LETTERS
卷 591, 期 8, 页码 1073-1082

出版社

WILEY
DOI: 10.1002/1873-3468.12529

关键词

genetic recombination

资金

  1. Biotechnology and Biological Sciences Research Council [B17092, BB/P001491/1, BB/E001777/1] Funding Source: researchfish
  2. Cancer Research UK [11722, 18604] Funding Source: researchfish
  3. Engineering and Physical Sciences Research Council [EP/J017094/1] Funding Source: researchfish
  4. BBSRC [BB/E001777/1, BB/P001491/1] Funding Source: UKRI
  5. Biotechnology and Biological Sciences Research Council [BB/E001777/1, B17092] Funding Source: Medline
  6. Cancer Research UK [11722] Funding Source: Medline

向作者/读者索取更多资源

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.

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