The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli

Biochem Biophys Res Commun. 2002 Dec 6;299(3):438-45. doi: 10.1016/s0006-291x(02)02660-8.

Abstract

The ZntR protein from Escherichia coli is a member of the MerR-family of transcriptional regulatory proteins and acts as a hyper-sensitive transcriptional switch primarily in response to Zn(II) and Cd(II). The binding of metal-ions to ZntR initiates a mechanism that remodels the cognate promoter, increasing its affinity for RNA polymerase. We have introduced site-directed mutations into zntR and shown that cysteine and histidine residues are important for transcriptional control and have an effect on metal-ion preference, sensitivity and magnitude of induction. We propose a three-dimensional model of the N-terminal region of ZntR based upon the coordinates of the MerR-family regulator BmrR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / metabolism*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • Genes, Reporter
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Promoter Regions, Genetic
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism
  • Transcription, Genetic

Substances

  • Amino Acids
  • Bacterial Proteins
  • Escherichia coli Proteins
  • Transcription Factors
  • ZntR protein, E coli
  • ZntR protein, bacteria