Structural and functional studies of a large winged Z-DNA-binding domain of Danio rerio protein kinase PKZ

FEBS Lett. 2016 Jul;590(14):2275-85. doi: 10.1002/1873-3468.12238. Epub 2016 Jun 23.

Abstract

The Z-DNA-binding domain of PKZ from zebrafish (Danio rerio; drZαPKZ ) contains the largest β-wing among known Z-DNA-binding domains. To elucidate the functional implication of the β-wing, we solved the crystal structure of apo-drZαPKZ . Structural comparison with its Z-DNA-bound form revealed a large conformational change within the β-wing during Z-DNA binding. Biochemical studies of protein mutants revealed that two basic residues in the β-wing are responsible for Z-DNA recognition as well as fast B-Z transition. Therefore, the extra basic residues in the β-wing of drZαPKZ are necessary for the fast B-Z transition activity.

Keywords: B-Z transition; PKZ; Z-DNA; Zα; zebrafish.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallography, X-Ray
  • DNA, Z-Form / chemistry
  • DNA, Z-Form / genetics
  • DNA, Z-Form / metabolism
  • Mutation
  • Protein Kinases / chemistry*
  • Protein Kinases / genetics
  • Protein Kinases / metabolism
  • Protein Structure, Secondary
  • Structure-Activity Relationship
  • Zebrafish Proteins / chemistry*
  • Zebrafish Proteins / genetics
  • Zebrafish Proteins / metabolism
  • Zebrafish*

Substances

  • DNA, Z-Form
  • Zebrafish Proteins
  • PKZ protein, zebrafish
  • Protein Kinases

Associated data

  • GENBANK/AAP49830.1
  • GENBANK/AJ852018.1