The Escherichia coli histone-like protein HU has a role in stationary phase adaptive mutation

Genetics. 2007 Oct;177(2):723-35. doi: 10.1534/genetics.107.075861. Epub 2007 Aug 24.

Abstract

Stationary phase adaptive mutation in Escherichia coli is thought to be a mechanism by which mutation rates are increased during stressful conditions, increasing the possibility that fitness-enhancing mutations arise. Here we present data showing that the histone-like protein, HU, has a role in the molecular pathway by which adaptive Lac(+) mutants arise in E. coli strain FC40. Adaptive Lac(+) mutations are largely but not entirely due to error-prone DNA polymerase IV (Pol IV). Mutations in either of the HU subunits, HUalpha or HUbeta, decrease adaptive mutation to Lac(+) by both Pol IV-dependent and Pol IV-independent pathways. Additionally, HU mutations inhibit growth-dependent mutations without a reduction in the level of Pol IV. These effects of HU mutations on adaptive mutation and on growth-dependent mutations reveal novel functions for HU in mutagenesis.

Publication types

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

MeSH terms

  • Adaptation, Physiological / genetics*
  • DNA Polymerase beta
  • DNA-Binding Proteins / genetics*
  • Escherichia coli Proteins / genetics*
  • Lac Operon
  • Mutation / physiology*
  • Protein Subunits / genetics

Substances

  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • Protein Subunits
  • hns protein, E coli
  • DNA Polymerase beta