Sequence discrimination of the Zα domain of human ADAR1 during B-Z transition of DNA duplexes

FEBS Lett. 2010 Oct 22;584(20):4344-50. doi: 10.1016/j.febslet.2010.09.036. Epub 2010 Sep 26.

Abstract

The Zα domain of human ADAR1 (Zα(ADAR1)) preferentially binds Z-DNA rather than B-DNA with high binding affinity. Zα(ADAR1) binds to the Z-conformation of both non-CG-repeat DNA duplexes and a d(CGCGCG)(2) duplex similarly. We performed NMR experiments on complexes between the Zα(ADAR1) and non-CG-repeat DNA duplexes, d(CACGTG)(2) or d(CGTACG)(2), with a variety of protein-DNA molar ratios. Comparison of these results with those from the analysis of d(CGCGCG)(2) in the previous study suggests that Zα(ADAR1) exhibits the sequence preference of d(CGCGCG)(2)≫d(CACGTG)(2)>d(CGTACG)(2) through multiple sequence discrimination steps during the B-Z transition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Deaminase / chemistry*
  • Adenosine Deaminase / genetics
  • Adenosine Deaminase / metabolism
  • Algorithms
  • Base Sequence
  • Binding Sites
  • Binding, Competitive
  • Calorimetry / methods
  • DNA / chemistry*
  • DNA / metabolism
  • DNA, Z-Form / chemistry*
  • DNA, Z-Form / metabolism
  • Humans
  • Kinetics
  • Magnetic Resonance Spectroscopy / methods
  • Models, Chemical
  • Nucleic Acid Conformation*
  • Oligonucleotides / chemistry
  • Oligonucleotides / metabolism
  • RNA-Binding Proteins

Substances

  • DNA, Z-Form
  • Oligonucleotides
  • RNA-Binding Proteins
  • DNA
  • ADARB1 protein, human
  • Adenosine Deaminase