Regulation of Salmonella enterica pathogenicity island 1 (SPI-1) by the LysR-type regulator LeuO

Mol Microbiol. 2014 Mar;91(6):1057-69. doi: 10.1111/mmi.12500. Epub 2014 Jan 13.

Abstract

LeuO is a quiescent LysR-type regulator belonging to the H-NS regulon. Activation of leuO transcription represses expression of pathogenicity island 1 (SPI-1) in Salmonella enterica serovar Typhimurium and inhibits invasion of epithelial cells. Loss of HilE suppresses LeuO-mediated downregulation of SPI-1. Activation of leuO transcription reduces the level of HilD protein, and loss of HilE restores the wild type HilD level. Hence, LeuO-mediated downregulation of SPI-1 may involve inhibition of HilD activity by HilE, a view consistent with the fact that HilE is a HilD inhibitor. In vivo analyses using β-galactosidase fusions indicate that LeuO activates hilE transcription. In vitro analyses by slot blotting, electrophoretic mobility shift analysis and DNase I footprinting show that LeuO binds the hilE promoter region. Although residual SPI-1 repression by LeuO is observed in the absence of HilE, the LeuO-HilE-HilD 'pathway' appears to be the major mechanism. Because both leuO and SPI-1 are repressed by H-NS, activation of leuO transcription may provide a backup mechanism for SPI-1 repression under conditions that impair H-NS-mediated silencing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Artificial Gene Fusion
  • Bacterial Proteins / biosynthesis*
  • Bacterial Proteins / genetics
  • DNA Footprinting
  • Electrophoretic Mobility Shift Assay
  • Gene Expression Regulation, Bacterial*
  • Genes, Reporter
  • Genomic Islands*
  • Promoter Regions, Genetic
  • Repressor Proteins / biosynthesis*
  • Repressor Proteins / genetics
  • Salmonella typhimurium / genetics*
  • Transcription Factors / metabolism*
  • Virulence Factors / genetics*
  • beta-Galactosidase / analysis
  • beta-Galactosidase / genetics

Substances

  • Bacterial Proteins
  • Repressor Proteins
  • Transcription Factors
  • Virulence Factors
  • beta-Galactosidase