Basis of dATP inhibition of RNRs

J Biol Chem. 2018 Jun 29;293(26):10413-10414. doi: 10.1074/jbc.H118.003717.

Abstract

Ribonucleotide reductases (RNRs) are essential enzymes producing de novo deoxynucleotide (dNTP) building blocks for DNA replication and repair and regulating dNTP pools important for fidelity of these processes. A new study reveals that the class Ia Escherichia coli RNR is regulated by dATP via stabilization of an inactive α4β4 quaternary structure, slowing formation of the active α2β2 structure. The results support the importance of the regulatory α4β4 complex providing insight in design of experiments to understand RNR regulation in vivo.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Allosteric Regulation / drug effects
  • Catalytic Domain
  • Deoxyadenine Nucleotides / pharmacology*
  • Escherichia coli / enzymology
  • Models, Molecular
  • Ribonucleotide Reductases / antagonists & inhibitors*
  • Ribonucleotide Reductases / chemistry
  • Ribonucleotide Reductases / metabolism

Substances

  • Deoxyadenine Nucleotides
  • Ribonucleotide Reductases
  • 2'-deoxyadenosine triphosphate