Identical, independent, and opposing roles of ppGpp and DksA in Escherichia coli

J Bacteriol. 2007 Jul;189(14):5193-202. doi: 10.1128/JB.00330-07. Epub 2007 May 11.

Abstract

The recent discovery that the protein DksA acts as a coregulator of genes controlled by ppGpp led us to investigate the similarities and differences between the relaxed phenotype of a ppGpp-deficient mutant and the phenotype of a strain lacking DksA. We demonstrate that the absence of DksA and ppGpp has similar effects on many of the observed phenotypes but that DksA and ppGpp also have independent and sometimes opposing roles in the cell. Specifically, we show that overexpression of DksA can compensate for the loss of ppGpp with respect to transcription of the promoters P(uspA), P(livJ), and P(rrnBP1) as well as amino acid auxotrophy, cell-cell aggregation, motility, filamentation, and stationary phase morphology, suggesting that DksA can function without ppGpp in regulating gene expression. In addition, ppGpp and DksA have opposing effects on adhesion. In the course of our analysis, we also discovered new features of the relaxed mutant, namely, defects in cell-cell aggregation and motility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / metabolism
  • Bacterial Adhesion / genetics
  • Bacterial Adhesion / physiology
  • Blotting, Western
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Escherichia coli / ultrastructure
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism
  • Escherichia coli Proteins / physiology
  • Gene Expression Regulation, Bacterial
  • Guanosine Tetraphosphate / metabolism*
  • Guanosine Tetraphosphate / physiology
  • Microscopy, Electron, Scanning
  • Models, Biological
  • beta-Galactosidase / genetics
  • beta-Galactosidase / metabolism

Substances

  • Amino Acids
  • Escherichia coli Proteins
  • dksA protein, E coli
  • Guanosine Tetraphosphate
  • beta-Galactosidase