Phosphorylated DegU Manipulates Cell Fate Differentiation in the Bacillus subtilis Biofilm

Victoria L. Marlow, Michael Porter, Laura Hobley, Taryn B. Kiley, Jason R. Swedlow, Fordyce A. Davidson, Nicola R. Stanley-Wall

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)

Abstract

Cell differentiation is ubiquitous and facilitates division of labor and development. Bacteria are capable of multicellular behaviors that benefit the bacterial community as a whole. A striking example of bacterial differentiation occurs throughout the formation of a biofilm. During Bacillus subtilis biofilm formation, a subpopulation of cells differentiates into a specialized population that synthesizes the exopolysaccharide and the TasA amyloid components of the extracellular matrix. The differentiation process is indirectly controlled by the transcription factor Spo0A that facilitates transcription of the eps and tapA (tasA) operons. DegU is a transcription factor involved in regulating biofilm formation. Here, using a combination of genetics and live single-cell cytological techniques, we define the mechanism of biofilm inhibition at high levels of phosphorylated DegU (DegU∼P) by showing that transcription from the eps and tapA promoter regions is inhibited. Data demonstrating that this is not a direct regulatory event are presented. We demonstrate that DegU∼P controls the frequency with which cells activate transcription from the operons needed for matrix biosynthesis in favor of an off state. Subsequent experimental analysis led us to conclude that DegU∼P functions to increase the level of Spo0A∼P, driving cell fate differentiation toward the terminal developmental process of sporulation.

Original languageEnglish
Pages (from-to)16-27
Number of pages12
JournalJournal of Bacteriology
Volume196
Issue number1
DOIs
Publication statusPublished - Jan 2014

Keywords

  • Bacillus subtilis
  • Bacterial Proteins
  • Biofilms
  • Cytological Techniques
  • Gene Expression Regulation, Bacterial
  • Molecular Biology
  • Phosphorylation
  • Protein Processing, Post-Translational

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