Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair

  • Dalhus B
  • Arvai A
  • Rosnes I
 et al. 
  • 44

    Readers

    Mendeley users who have this article in their library.
  • 54

    Citations

    Citations of this article.

Abstract

Endonuclease V (EndoV) initiates a major base-repair pathway for nitrosative deamination resulting from endogenous processes and increased by oxidative stress from mitochondrial dysfunction or inflammatory responses. We solved the crystal structures of Thermotoga maritima EndoV in complex with a hypoxanthine lesion substrate and with product DNA. The PYIP wedge motif acts as a minor groove-damage sensor for helical distortions and base mismatches and separates DNA strands at the lesion. EndoV incises DNA with an unusual offset nick 1 nucleotide 3' of the lesion, as the deaminated adenine is rotated approximately 90 degrees into a recognition pocket approximately 8 A from the catalytic site. Tight binding by the lesion-recognition pocket in addition to Mg(2+) and hydrogen-bonding interactions to the DNA ends stabilize the product complex, suggesting an orderly recruitment of downstream proteins in this base-repair pathway.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Bjørn Dalhus

  • Andrew S. Arvai

  • Ida Rosnes

  • Øyvind E. Olsen

  • Paul H. Backe

  • Ingrun Alseth

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free