Flagella-independent surface motility in Salmonella enterica serovar Typhimurium

Proc Natl Acad Sci U S A. 2015 Feb 10;112(6):1850-5. doi: 10.1073/pnas.1422938112. Epub 2015 Jan 26.

Abstract

Flagella are multiprotein complexes necessary for swimming and swarming motility. In Salmonella enterica serovar Typhimurium, flagella-mediated motility is repressed by the PhoP/PhoQ regulatory system. We now report that Salmonella can move on 0.3% agarose media in a flagella-independent manner when experiencing the PhoP/PhoQ-inducing signal low Mg(2+). This motility requires the PhoP-activated mgtA, mgtC, and pagM genes, which specify a Mg(2+) transporter, an inhibitor of Salmonella's own F1Fo ATPase, and a small protein of unknown function, respectively. The MgtA and MgtC proteins are necessary for pagM expression because pagM mRNA levels were lower in mgtA and mgtC mutants than in wild-type Salmonella, and also because pagM expression from a heterologous promoter rescued motility in mgtA and mgtC mutants. PagM promotes group motility by a surface protein(s), as a pagM-expressing strain conferred motility upon a pagM null mutant, and proteinase K treatment eliminated motility. The pagM gene is rarely found outside subspecies I of S. enterica and often present in nonfunctional allelic forms in organisms lacking the identified motility. Deletion of the pagM gene reduced bacterial replication on 0.3% agarose low Mg(2+) media but not in low Mg(2+) liquid media. Our findings define a form of motility that allows Salmonella to scavenge nutrients and to escape toxic compounds in low Mg(2+) semisolid environments.

Keywords: MgtA; MgtC; PagM; PhoP/PhoQ; magnesium.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Cation Transport Proteins / metabolism*
  • Computational Biology
  • Flagella / metabolism
  • Gene Expression Regulation, Bacterial / physiology*
  • Magnesium / metabolism
  • Membrane Transport Proteins / metabolism*
  • Mitochondrial Proton-Translocating ATPases / antagonists & inhibitors
  • Molecular Sequence Data
  • Movement / physiology*
  • Mutagenesis
  • Salmonella typhimurium / physiology*
  • Sequence Alignment
  • Sequence Analysis, DNA

Substances

  • Bacterial Proteins
  • Cation Transport Proteins
  • Membrane Transport Proteins
  • PhoQ protein, Bacteria
  • PhoP protein, Bacteria
  • Adenosine Triphosphatases
  • F1F0-ATP synthase
  • MgtA protein, bacteria
  • MgtC protein, Salmonella typhimurium
  • Mitochondrial Proton-Translocating ATPases
  • Magnesium