The LuxR family quorum-sensing activator MrtR requires its cognate autoinducer for dimerization and activation but not for protein folding

J Bacteriol. 2009 Jan;191(1):434-8. doi: 10.1128/JB.01247-08. Epub 2008 Oct 31.

Abstract

MrtR, a LuxR homolog in Mesorhizobium tianshanense, is important for symbiosis. We found that MrtR requires its cognate N-acylhomoserine lactone for forming dimers, binding to a single DNA site and activating the downstream promoter. However, MrtR is able to fold independently of its ligand.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agrobacterium tumefaciens / genetics
  • Bacterial Proteins / metabolism
  • Base Sequence
  • DNA, Bacterial / genetics
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / physiology*
  • Dimerization
  • Molecular Sequence Data
  • Mutagenesis
  • Plasmids
  • Protein Folding
  • Quorum Sensing / genetics
  • Quorum Sensing / physiology*
  • Repressor Proteins / genetics
  • Repressor Proteins / physiology*
  • Rhizobium / physiology*
  • Symbiosis / physiology
  • Trans-Activators / genetics
  • Trans-Activators / physiology*

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • Repressor Proteins
  • Trans-Activators
  • LuxR autoinducer binding proteins